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MITF in melanoma: mechanisms behind its expression and activity

Mariusz L. Hartman, Malgorzata Czyz

Cellular and Molecular Life Sciences · 2014 · Review

doi:10.1007/s00018-014-1791-0

Abstract

MITF (microphthalmia-associated transcription factor) represents a melanocytic lineage-specific transcription factor whose role is profoundly extended in malignant melanoma. Over the last few years, the function of MITF has been tightly connected to plasticity of melanoma cells. MITF participates in executing diverse melanoma phenotypes defined by distinct gene expression profiles. Mutation-dependent alterations in MITF expression and activity have been found in a relatively small subset of melanomas. MITF activity is rather modulated by its upstream activators and suppressors operating on transcriptional, post-transcriptional and post-translational levels. These regulatory mechanisms also include epigenetic and microenvironmental signals. Several transcription factors and signaling pathways involved in the regulation of MITF expression and/or activity such as the Wnt/β-catenin pathway are broadly utilized by various types of tumors, whereas others, e.g., BRAF(V600E)/ERK1/2 are more specific for melanoma. Furthermore, the MITF activity can be affected by the availability of transcriptional co-partners that are often redirected by MITF from their own canonical signaling pathways. In this review, we discuss the complexity of a multilevel regulation of MITF expression and activity that underlies distinct context-related phenotypes of melanoma and might explain diverse responses of melanoma patients to currently used therapeutics.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 18, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

Melanocytes are pigment-producing cells whose differentiation, proliferation and survival largely depend on MITF (microphthalmia-associated transcription factor), a melanocyte-specific transcription factor [for review, ]. Melanoma is a melanocyte-derived tumor in which MITF dependence is retained [for review ]; thus, MITF represents a lineage-restricted regulator that operates in normal cells, and its activity is also used by malignant cells. Enforced expression of MITF in immortalized melanocytes or neural crest progenitor cells when introduced together with melanoma-specific BRAFV600E suggests MITF’s role as a melanoma addiction oncogene. MITF is recognized as a driver of melanoma progression [for review ], but its role in suppression of invasion and metastasis has been also shown. By activating the expression of almost one hundred genes, MITF can regulate multiple biological processes in melanoma cells such as differentiation, proliferation, migration, and senescence [–; for review, ]. MITF also exerts pro-survival role by activating the expression of anti-apoptotic genes including BCL2A1, BCL2 and BIRC7 (ML-IAP/livin) [for review, ]. Recent studies implicate MITF in energy metabolism and organelle biogenesis [; for review ]. This variety of often mutually exclusive cellular programs driven by MITF stands for distinct phenotypes of melanoma cells [,,; for review, ]. MITF is also recognized as a major regulator in a “phenotypic switching” concept explaining a high plasticity of melanoma cells [,, –; for review, ]. Therefore, better understanding of the intracellular mechanisms underlying a contextual regulation of MITF is of utmost importance. In this review, we focus on melanoma-related mechanisms underlying the regulation of MITF expression and activity.

Gene structure and transcriptional regulation of MITF

In human, MITF locus is mapped to chromosome 3 and spans 229 kbp. MITF encodes a b-HLH-Zip (basic helix-loop-helix leucine zipper) transcription factor that belongs to the MYC superfamily. Together with TFEB, TFEC and TFE3, MITF constitutes the MiT (microphthalmia) family of transcription factors. All of them share a common b-HLH-Zip dimerization motif containing a positively charged fragment involved in DNA binding, and a transactivation domain (TAD). As a result of differential usage of alternative promoters, a single MITF gene produces several isoforms including MITF-A, MITF-B, MITF-C, MITF-D, MITF-E, MITF-H, MITF-J, MITF-Mc and MITF-M. These isoforms differ in their N-termini encoded by exon 1, and show tissue-specific pattern of expression. The expression of the shortest isoform MITF-M (a 419-residue protein) is limited to melanocytes and melanoma cells [; for review ]. MITF-Mdel, a variant of MITF-M harboring two in-frame deletions within the exons 2 and 6, has been identified as restrictedly expressed in these cells. MITF contains two TADs responsible for its transcriptional activity; however, a functional domination of the TAD at N-terminus over that one at C-terminus has been reported. MITF binds to DNA as a homodimer or heterodimer with one of the MiT proteins, but does not form heterodimers with other b-HLH-Zip transcription factors such as MYC, MAX and USF, despite a common ability to bind to the palindromic CACGTG E-box motif. It was shown that the heptad repeat register of the leucine zipper in MITF is broken by a three-residue insertion that generates a kink in one of the two zipper helices, which limits the ability of MITF to form dimers only with those bHLHZip transcription factors that contain the same type of insertion. Functionally, the MITF-binding sites in the promoters of target genes involve E-box: CA[C/T]GTG and M-box, extended E-box with an additional 5′-end flanking thymidine nucleotide: TCATGTGCT [for review ].

Genetic alterations in MITF and alternative splicing

Some genetic alterations have been associated with MITF. Initially, high-density single nucleotide polymorphism arrays revealed the MITF amplification in up to 20 % of melanomas, with higher incidence among metastatic melanoma samples. This aberration correlated with decreased overall patient survival. However, in a recent study involving targeted-capture deep sequencing, no copy gains at the MITF locus have been found in a panel of melanoma metastases. Genetic abnormalities related to MITF also include single base substitutions in the regions encoding its functional domains. These somatic mutations, however, do not affect the DNA-binding ability of MITF in melanoma cells. Recently, two independent studies have identified a rare oncogenic MITFE318K variant representing a gain-of-function allele for MITF that is present in patients with familial melanoma and a small fraction of sporadic melanomas. MITF E318K has been described as a medium-penetrance gene in melanoma associated with multiple primary melanomas developed in its carriers, and as predisposing to renal carcinoma as well.

Alternative splicing is another mechanism of MITF regulation in melanoma. Two spliced variants of MITF, MITF(+) containing an internal six-amino acid fragment encoded by exon 6a and MITF(−) that lacks this fragment, have been described. These two variants possess different activity, with anti-proliferative property of MITF(+). This effect is tightly related to the interaction between the N-terminal fragment of MITF(+) with its specific hexapeptide. Activation of the MEK1-ERK2 (extracellular signal-regulated kinase 2) pathway, independently of the mutational status of BRAF and NRAS, has been indicated as a mechanism underlying the expression of MITF splice variants. Additionally, the quantification of these variants in a panel of 86 melanoma samples revealed the apparently increased expression of MITF(−) in metastatic melanomas.

Transcriptional activators of MITF

The transcriptional control of MITF is governed by a number of transcription factors and their regulators associated with signaling pathways involved in diverse cellular processes (Fig. 1). SOX10 (sex-determining region Y-box 10)-responsive element was found between −264 and −266 in the MITF promoter. In addition, an activating frameshift or non-sense mutations in SOX10 have been identified in melanoma cells, and MITF and SOX10 have been found mutated in a mutually exclusive manner. The nuclear localization of SOX10 is maintained by a protein tyrosine kinase TYRO3. SOX10 also cooperates with CREB (cAMP response element-binding protein) in the responsiveness of MITF to α-MSH (α-melanocyte-stimulating hormone)-cAMP signaling. This constitutes a tightly restricted mechanism of regulation due to a ubiquitous expression of CREB and a cell type-limited expression of SOX10. CREB is targeted by a number of regulators that promote its phosphorylation at Ser133, thus activating CREB-dependent transcription (Fig. 1) [; for review ]. It has been demonstrated that p38, activated by either UV (ultraviolet radiation) or receptors, e.g., KIT, phosphorylates CREB and promotes its binding to the MITF promoter. p21Cip1, a cell cycle inhibitor, has been identified as a CREB co-factor involved in cAMP-dependent MITF expression in melanoma. MITF expression can be also mediated by the complex of two key effectors of the Wnt (wingless-type) signaling pathway, LEF1 (lymphoid enhancer-binding factor 1) and β-catenin. In contrast to β-catenin, a phenotype-specific expression of LEF1 has been shown in melanoma cells limiting LEF1/β-catenin-dependent MITF transcription to a defined cellular context. Importantly, MITF can cooperate with LEF1 as a non-DNA-binding coactivator to enhance its own expression. It has been also demonstrated that mediators of α-MSH/cAMP/PKA (protein kinase A) signaling can redirect β-catenin to the CREB-specific promoters to activate transcription of CREB target genes including MITF. Most recently, a transcription factor involved in epithelial–mesenchymal transition [; for review, ], ZEB2 (zing finger E-box binding protein 2) has been shown to activate MITF expression, and a ZEB2 loss that resulted in a decreased MITF level and several MITF-dependent target genes was associated with melanoma progression. In contrast to activating potential of ZEB2 on the MITF promoter, ZEB1 has been found to directly repress MITF expression in retinal pigment epithelium. Thus, the role of ZEB1 in the context of MITF expression in melanoma needs to be elucidated. On the level of chromatin remodeling, it has been demonstrated that a SWI/SNF complex containing BRM (Brahma) or BRG1 (Brahma-related gene 1) promotes MITF expression.

Transcriptional repressors of MITF

Several transcription factors have been identified as direct repressors of MITF (Fig. 1). Inverse expression of GLI2 (glioma-associated oncogene family member 2) and MITF-M, relating to the mutually exclusive transcriptional programs, has been observed in melanoma cells. GLI2 is a Kruppel-like transcription factor activated by TGFβ (transforming growth factor β). Furthermore, a GLI2 binding site was identified in the −334/−296 region of the MITF promoter confirming direct inhibitory activity of GLI2 towards MITF. The contribution of PAX3 (paired box 3) to MITF expression represents another melanoma-specific mechanism. Although positive regulation of MITF by PAX3 in melanocytes is well described, PAX3 is thought to function independently of MITF or even play a repressive role on MITF expression in melanoma. PAX3 is activated by PI3 K (phosphatidylinositol 3-kinase) and STAT3 (signal transducer and activator of transcription 3) in melanoma cells, and a negative PAX3-dependent regulation of MITF expression is mediated by BRN2 encoded by POU3F2. Notably, BRN2-mediated repression of MITF transcription represents a mechanism distinguishing between melanoma cells and melanocytes due to the lack of BRN2 expression in the latter, which might be explained by the involvement of melanoma-specific BRAFV600E in BRN2 upregulation. Moreover, inverse expression of MITF and BRN2 was shown in vitro and in vivo. The antagonistic MITF and PAX3 expression has been proposed as a switch model in which MITF and miR-211, residing in the sixth intron of TRPM1, can activate one cellular program while suppressing another one driven by PAX3 and BRN2. MITF repression is also mediated by DEC1 (differentially expressed in chondrocytes protein 1) whose recruitment to the MITF promoter is regulated by HIF1 (hypoxia-inducible factor 1). As HIF1α is a MITF target and can be expressed in melanoma cells not only under hypoxic conditions, this mechanism constitutes an interesting negative feedback loop regulating MITF expression.

Several proteins have been found to indirectly suppress MITF expression by acting as upstream inhibitors of positive regulators of MITF expression (Fig. 1). Independently of its effect on GLI2, TGFβ inhibits PKA that otherwise promotes CREB-dependent MITF transcription. DKK1 (Dickkopf-1), a secreted inhibitor of the Wnt/β-catenin pathway, has been shown to suppress both MITF expression and the MITF-dependent differentiation program. Accordingly, both DKK1 expression and secretion have been substantially reduced in the multicellular anchorage-independent melanospheres showing high expression of MITF and numerous MITF target genes. ATF2 (activating transcription factor 2) displays inhibitory activity towards SOX10 both in melanocytes and melanoma cells, resulting in a decreased MITF transcript level. A co-immunoprecipitation approach confirmed selective affinity of BCSC1 (breast cancer suppressor candidate-1) to SOX10, but not other MITF regulators such as CREB, and down-regulated MITF mRNA level was observed upon BCSC-1 overexpression. MITF expression is also affected by IFN-γ (interferon γ) that inhibits CREB binding to the MITF promoter by inducing the association of CBP (CREB binding protein) with STAT1.

Regulation of MITF transcript stability

Melanoma cells show high expression of CRD-BP (coding region determinant-binding protein), an mRNA-binding protein that has been found to stabilize MITF transcript. MITF transcript is also under control of several small non-coding RNAs, microRNAs (miRs), which promote mRNA degradation or suppress protein synthesis via binding to 3′-UTR of a target transcript. miR-137, located in the locus 1p22, negatively regulates MITF. No mutations have been found in the putative miR-137-binding sites in the MITF mRNA 3′-UTR, however, miR-137 possesses a 15-bp tandem repeat in the pre-miR-137 sequence that alters the processing and function of miR-137 in melanoma cell lines. In metastatic melanoma samples, MITF transcript has been determined as a target of miR-182-mediated degradation. miR-182 is a member of the miR cluster residing in a chromosomal locus (7q31–34) frequently amplified in melanomas. Interestingly, overexpression of MITF has been related to the suppression of the miR-182-dependent pro-invasive effect. p53-dependent miR-182 has been also found to down-regulate MITF in uveal melanoma. The 3′-UTR of MITF transcript is also targeted by miR-148, miR-101 and miR-218, and inverse correlation between MITF and miR-218 has been observed in melanocytes and melanoma cell lines. Notably, exosome-dependent miR exchange between melanoma cells may influence MITF transcript level as well [for review ].

Regulation of MITF protein level and activity

The transcriptional activity of MITF depends on its post-translational modifications and availability of co-operating partners (Fig. 2). MITF can be regulated by phosphorylation maintained by ERK1/2 (at Ser73), p90RSK (at Ser409), GSK3β (at Ser298) and p38 (at Ser307). In general, phosphorylation enhances transcriptional activity of MITF [,; for review ]. The phosphorylation at Ser73 promotes the interaction with a MITF co-factor, histone acetyl transferase p300/CBP within the transactivation domain of MITF. On the other hand, this modification promotes the binding of PIAS3 (protein inhibitor of activated STAT3) that involves the N-terminal fragment of PIAS3 and the leucine zipper of MITF. Interaction with PIAS3 leads to the attenuation of MITF transcriptional activity. This effect is, however, inhibited when MITF is phosphorylated at Ser409 in a p90RSK-dependent manner. The phosphorylation of MITF at Ser73, a residue located within a degradation-promoting PEST sequence, is also a prerequisite to the MITF proteasome-dependent turnover e.g., in response to ultraviolet C radiation. Lys201 has been identified as a site of UBC9-mediated ubiquitylation of MITF. Proteasome-mediated MITF protein degradation has also been observed after double phosphorylation at Ser73 and Ser409. An unphosphorylatable mutant at Ser73/Ser409 has been very stable but transcriptionally incompetent, indicating that signals promoting transcriptional activity and degradation of MITF protein are coupled in melanoma cells. Both phosphorylations promoting MITF degradation depend on melanoma-specific BRAFV600E causing the enhanced activation of MAPK (MAP kinase)/ERK1/2 pathway. Deubiquitinase USP13 (ubiquitin-specific protease 13) has been linked to the protection of MITF from proteasomal degradation in melanoma cells. MITF can be also processed by the effector caspases. It has been demonstrated in melanoma cells that MITF-derived C-terminal peptide cleaved by these proteases has a pro-apoptotic function.

MITF activity is also modulated by SUMOylation at two lysine residues, Lys182 and Lys316. SUMOylation of MITF depends on an E1 SUMO-activating heterodimeric enzyme SAEI/SAEII and E2 SUMO-conjugating enzyme UBC9 (Fig. 2). It has been concluded that this modification plays an essential role in the regulation of MITF activity, and non-SUMOylatable MITF mutants displayed increased transcriptional activity on distinct sets of target genes. It has been also indicated that PIAS3 can promote MITF SUMOylation at both SUMOylation sites; however, this observation has not been clearly supported by another report. A recent study on melanoma patients bearing the MITFE318K variant, in which a point mutation occurs at the consensus binding site for SUMOylation, supports the conclusion that this substitution does not affect MITF protein stability and nuclear localization.

Besides aforementioned regulations, MITF activity also depends on the availability of co-operating partners such as p300/CBP. p300/CBP is a versatile regulator that links transcription factors bound to DNA with a basal transcriptional machinery, thus promoting the assembly of pre-initiation complex [for review ]. Immunofluorescence and immunoprecipitation studies have demonstrated that MITF can physically interact with BRM and BRG1, and depending on the type of SWI/SNF complex composed of either the BRG1 or BRM subunit, different sets of MITF-dependent genes are activated. This, however, is not an exclusive role of the BRG1-containing SWI/SNF complex in melanoma since its MITF-independent activity has been shown as well. SOX10 can synergistically activate the MITF-dependent genes as demonstrated for MET. It has been also shown that MITF can redirect β-catenin from the Wnt signaling pathway, and engage it to the activation of MITF-dependent genes. Thus, SWI/SNF complex, SOX10 and β-catenin can function not only as activators of MITF expression (Fig. 1), but also as its co-factors. HINT1 (histidine triad nucleotide-binding protein 1) has been identified as an inhibitor of transcriptional activity of MITF acting through binding the chromatin at the MITF sites. Moreover, since HINT1 expression is lost in primary melanomas, it may support a role of MITF in melanomagenesis.

The mechanisms behind the regulation of MITF level and activity are still being explored. Most recently, very interesting correlations have been observed between activity of MITF and other transcription factors, probably not operating on the MITF promoter (Fig. 1). HOXA1 (homeobox transcription factor 1) has been identified as a potent inhibitor of MITF expression whose activity might be concomitant with the activation of the TGFβ pathway. An interesting repression mechanism has been reported in melanoma cells expressing IL-1R (interleukin-1 receptor). The stimulation of melanoma cells with interleukin-1α or 1β resulted in the reduction of MITF expression, and it has been suggested that this process is NF-κB-dependent. Accordingly, a suppressive role of the NF-κB signaling on MITF level has been reported. A reverse correlation has been observed between MYC-related chromosomal copy number gains in 8q24 and MITF expression. In contrast, suppression of ETV1 (E twenty-six variant 1) was associated with a decreased level of MITF protein. Whether c-MYC and ETV1 can act as direct regulators of MITF remains to be elucidated. Other poorly characterized regulators have been associated with MITF level, and the detailed mechanisms of their actions need to be clarified. PRMT5 (protein arginine methyltransferase 5) is an enzyme involved in post-translational protein modifications. PRMT5 expression has been found to be increased in melanoma, and siRNA-mediated depletion of PRMT5 resulted in a substantial decrease in the level of MITF protein indicating a positive regulatory effect. A similar influence on the MITF level has been demonstrated for PDE4D (phosphodiesterase subtype 4D), and PDE4D-depleted cells have shown a decreased MITF transcript level.

Final conclusions

MITF operates within a wide range of activity levels determining melanoma cell fate (Fig. 3) [, –; for review,, ]. Melanoma cells expressing MITF at high level can either differentiate or proliferate. Low activity of MITF is related to stem cell-like or invasive potential. Finally, long-term MITF suppression drives cell senescence. Although genetic alterations, including mutations and amplification of MITF, are found in melanoma samples, fluctuating MITF activity in melanoma cells is rather due to microenvironmental cues, critical epigenetic states and modifications of upstream signaling pathways. Different combinations of those factors determine transcriptional activity of MITF which in turn contributes to diverse cellular capabilities. This may explain a variable MITF expression across melanoma specimens but also between different areas of individual tumor samples reflecting both inter-tumoral heterogeneity and diversity of melanoma cell subpopulations comprising a tumor mass [,; for review ].

MITF does not exhibit a druggable target, and MITF-aimed approaches are thought to be rather based on the modulation of its upstream regulatory pathways. A number of natural and synthetic compounds have been used to modify MITF activity. A few natural compounds that either reduced or increased MITF transcript level in heterogeneous patient-derived melanoma populations were identified in our laboratory. A dietary flavonoid fisetin that targets Wnt/β-catenin pathway has substantially reduced MITF expression and influenced MITF-dependent cellular processes. Downregulation of MITF at the transcriptional level was observed for ciglitazone that also showed anti-melanoma effects in vivo. Hirsein A reduced the expression of MITF by modulating the expression of diverse components of MAPK signaling pathway. Several studies have linked a high MITF level with the resistance to MAPK-pathway inhibitors [,; for review –]. MITF targets are up-regulated by MAPK-pathway inhibitors, and enforced expression of MITF in BRAFV600E melanoma cells promotes resistance towards inhibitors of RAF, MEK and ERK [for review ]. As MITF expression can be reduced by histone deacetylase inhibitors (HDACi), combined HDAC and MAPK inhibition was shown to prevent MITF-driven resistance in melanoma cells. Another study suggests, however, that intrinsically resistant melanomas can be characterized by low expression/activity of MITF accompanied by enhanced activity of NF-κB signaling, and BRAF inhibition in MITF-high, drug-sensitive cells induces a transition to the MITF-low/NF-κB–high state. Most recent findings that modulation of MITF activity can drive phenotype switching in vivo, and abrogating MITF activity in melanoma leads to tumor regression, but a low level of wild-type MITF is oncogenic indicate that further studies are needed.

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    Not in our library10.1006/bbrc.1998.8838

  31. 31.

    Udono T, Yasumoto K, Takeda K, Amae S, Watanabe K, Saito H, Fuse N, Tachibana M, Takahashi K, Tamai M, Shibahara S. Structural organization of the human microphthalmia-associated transcription factor gene containing four alternative promoters. Biochim Biophys Acta. 2000;1491(1–3):205-219.

    Not in our library10.1016/s0167-4781(00)00051-8

  32. 32.

    Fuse N, Yasumoto KI, Takeda K, Amae S, Yoshizawa M, Udono T, Takahashi K, Tamai M, Tomita Y, Tachibana M, Shibahara S. Molecular cloning of cDNA encoding a novel microphthalmia-associated transcription factor isoform with a distinct amino-terminus. J Biochem. 1999;126(6):1043-1051.

    Not in our library10.1093/oxfordjournals.jbchem.a022548

  33. 33.

    Takeda K, Yasumoto K, Kawaguchi N, Udono T, Watanabe K, Saito H, Takahashi K, Noda M, Shibahara S. Mitf-D, a newly identified isoform, expressed in the retinal pigment epithelium and monocyte-lineage cells affected by Mitf mutations. Biochim Biophys Acta. 2002;1574(1–3):15-23.

    Not in our library10.1016/s0167-4781(01)00339-6

  34. 34.

    Oboki K, Morii E, Kataoka TR, Jippo T, Kitamura Y. Isoforms of mi transcription factor preferentially expressed in cultured mast cells of mice. Biochim Biophys Res Commun. 2002;290(4):1250-1254.

    Not in our library10.1006/bbrc.2002.6332

  35. 35.

    Steingrimsson E, Moore KJ, Lamoreux ML, Ferre-D’Amare AR, Burley SK, Zimring DC, Skow LC, Hodgkinson CA, Arnheiter H, Copeland NG, Jenkins NA. Molecular basis of mouse microphthalmia (mi) mutations helps explain their developmental and phenotypic consequences. Nat Genet. 1994;8(3):256-263.

    Not in our library10.1038/ng1194-256

  36. 36.

    Hershey CL, Fisher DE. Genomic analysis of the Microphthalmia locus and identification of the MITF-J/Mitf-J isoform. Gene. 2005;347(1):73-82.

    Not in our library10.1016/j.gene.2004.12.002

  37. 37.

    Takemoto CM, Yoon YJ, Fisher DE. The identification and functional characterization of a novel mast cell isoform of the microphthalmia-associated transcription factor. J Biol Chem. 2002;277(33):30244-30252.

    Not in our library10.1074/jbc.m201441200

  38. 38.

    Hodgkinson CA, Moore KJ, Nakayama A, Steingrímsson E, Copeland NG, Jenkins NA, Arnheiter H. Mutations at the mouse microphthalmia locus are associated with defects in a gene encoding a novel basic-helix-loop-helix-zipper protein. Cell. 1993;74(2):395-404.

    Not in our library10.1016/0092-8674(93)90429-t

  39. 39.

    Tassabehji M, Newton VE, Read AP. Waardenburg syndrome type 2 caused by mutations in the human microphthalmia (MITF) gene. Nat Genet. 1994;8(3):251-255.

    Not in our library10.1038/ng1194-251

  40. 40.

    Widlund HR, Fisher DE. Microphthalmia-associated transcription factor: a critical regulator of pigment cell development and survival. Oncogene. 2003;22(20):3035-3041.

    Not in our library10.1038/sj.onc.1206443

  41. 41.

    Wang Y, Radfar S, Liu S, Riker AI, Khong HT. Mitf-Mdel, a novel melanocyte/melanoma-specific isoform of microphthalmia-associated transcription factor-M as a candidate biomarker for melanoma. BMC Med. 2010;8:14.

    Not in our library10.1186/1741-7015-8-14

  42. 42.

    Vachtenheim J, Drdova B. A dominant negative mutant of microphthalmia transcription factor (MITF) lacking two transactivation domains suppresses transcription mediated by wild type MITF and a hyperactive MITF derivative. Pigment Cell Res. 2004;17(1):43-50.

    Not in our library10.1046/j.1600-0749.2003.00108.x

  43. 43.

    Pogenberg V, Ogmundsdottir MH, Bergsteinsdottir K, Schepsky A, Phung B, Deineko V, Milewski M, Steingrimsson E, Wilmanns M. Restricted leucine zipper dimerization and specificity of DNA recognition of the melanocyte master regulator MITF. Genes Dev. 2012;26(23):2647-2658.

    Not in our library10.1101/gad.198192.112

  44. 44.

    Goding CR. Mitf from neural crest to melanoma: signal transduction and transcription in the melanocytic lineage. Genes Dev. 2000;14(14):1712-1728.

    Not in our library

  45. 45.

    Harbst K, Lauss M, Cirenajwis H, Winter C, Howlin J, Torngren T, Kvist A, Nodin B, Olsson E, Hakkinen J, Jirstrom K, Staaf J, Lundgren L, Olsson H, Ingvar C, Gruvberger-Saal SK, Saal LH, Jonsson G. Molecular and genetic diversity in the metastatic process of melanoma. J Pathol. 2014;233(1):39-50.

    Not in our library10.1002/path.4318

  46. 46.

    Cronin JC, Wunderlich J, Loftus SK, Prickett TD, Wei X, Ridd K, Vemula S, Burrell AS, Agrawal NS, Lin JC, Banister CE, Buckhaults P, Rosenberg SA, Bastian BC, Pavan WJ, Samuels Y. Frequent mutations in the MITF pathway in melanoma. Pigment Cell Melanoma Res. 2009;229(4):435-444.

    Not in our library10.1111/j.1755-148x.2009.00578.x

  47. 47.

    Grill C, Bergsteinsdottir K, Ogmundsdottir MH, Pogenberg V, Schepsky A, Wilmanns M, Pingault V, Steingrimsson E. MITF mutations associated with pigment deficiency syndromes and melanoma have different effects on protein function. Hum Mol Genet. 2013;22(21):4357-4367.

    Not in our library10.1093/hmg/ddt285

  48. 48.

    Bertolotto C, Lesueur F, Giuliano S, Strub T, de Lichy M, Bille K, Dessen P, d’Hayer B, Mohamdi H, Remenieras A, Maubec E, de la Fouchardiere A, Molinie V, Vabres P, Dalle S, Poulalhon N, Martin-Denavit T, Thomas L, Andry-Benzaquen P, Dupin N, Boitier F, Rossi A, Perrot JL, Labeille B, Robert C, Escudier B, Caron O, Brugieres L, Saule S, Gardie B, Gad S, Richard S, Couturier J, Teh BT, Ghiorzo P, Pastorino L, Puig S, Badenas C, Olsoon H, Ingvar C, Rouleau E, Lidereau R, Bahadoran P, Vielh P, Corda E, Blanche H, Zelenika D, Galan P, Aubin F, Bachollet B, Becuwe C, Berthet P, Bignon YJ, Bonadona V, Bonafe JL, Bonnett-Dupeyron MN, Cambazard F, Chevrant-Breton J, Coupier I, Dalac S, Demange L, d’Incan M, Dugast C, Faivre L, Vincent-Fetita L, Gauthier-Villars M, Gilbert B, Grange F, Grob JJ, Humbert P, Janin N, Joly P, Kerob D, Lasset C, Leroux D, Levang J, Limacher JM, Livideanu C, Longy M, Lortholary A, Stoppa-Lyonnet D, Mansard S, Mansuy L, Marrou K, Mateus C, Maugard C, Meyer N, Nogues C, Souteyrand P, Venat-Bouvet L, Zattara H, Chaudru V, Lenoir GM, Lathrop M, Davidson I, Avril MF, Demenais F, Ballotti R, Bressac-de-Paillerets B, French Familial Melanoma Study Group. A SUMOylation-defective MITF germline mutation predisposes to melanoma and renal carcinoma. Nature. 2011;480(7375):94-98.

    Not in our library10.1038/nature10539

  49. 49.

    Yokoyama S, Woods SL, Boyle GM, Aoude LG, MacGregor S, Zismann V, Gartside M, Cust AE, Haq R, Harland M, Taylor JC, Duffy DL, Holohan K, Dutton-Regester K, Palmer JM, Bonazzi V, Stark MS, Symmons J, Law MH, Schmidt C, Lanagan C, O’Connor L, Holland EA, Schmidt H, Maskiell JA, Jetann J, Ferguson M, Jenkins MA, Kefford RF, Giles GG, Armstrong BK, Aitken JF, Hopper JL, Whiteman DC, Pharoah PD, Easton DF, Dunning AM, Newton-Bishop JA, Montgomery GW, Martin NG, Mann GJ, Bishop DT, Tsao H, Trent JM, Fisher DE, Hayward NK, Brown KM. A novel recurrent mutation in MITF predisposes to familial and sporadic melanoma. Nature. 2011;480(7375):99-103.

    Not in our library10.1038/nature10630

  50. 50.

    Ghiorzo P, Pastorino L, Queirolo P, Bruno W, Tibiletti MG, Nasti S, Andreotti V, Paillerets BB, Bianchi Scarra G, Genoa Pancreatic Cancer Study Group. Prevalence of the MITF E318 K germline mutation in Italian melanoma patients: associations with histological subtypes and family cancer history. Pigment Cell Melanoma Res. 2013;26(2):259-262.

    Not in our library10.1111/pcmr.12047

  51. 51.

    Sturm RA, Fox C, McClenahan P, Jagirdar K, Ibarrola-Villava M, Banan P, Abbott NC, Ribas G, Gabrielli B, Duffy DL, Soyer HP. Phenotypic characterization of nevus and tumor patterns in MITF E318 K mutation carrier melanoma patients. J Invest Dermatol. 2014;134(1):141-149.

    Not in our library10.1038/jid.2013.272

  52. 52.

    Bismuth K, Maric D, Arnheiter H. MITF and cell proliferation: the role of alternative splice forms. Pigment Cell Res. 2005;18(5):349-359.

    Not in our library10.1111/j.1600-0749.2005.00249.x

  53. 53.

    Primot A, Mogha A, Corre S, Roberts K, Debbache J, Adamski H, Dreno B, Khammari A, Lesimple T, Mereau A, Goding CR, Galibert MD. ERK-regulated differential expression of the Mitf 6a/b splicing isoforms in melanoma. Pigment Cell Melanoma Res. 2010;23(1):93-102.

    Not in our library10.1111/j.1755-148x.2009.00652.x

  54. 54.

    Verastegui C, Bille K, Ortonne JP, Ballotti R. Regulation of the microphthalmia-associated transcription factor by the Waardenburg syndrome type 4 gene, SOX10. J Biol Chem. 2000;275(40):30757-30760.

    Not in our library10.1074/jbc.c000445200

  55. 55.

    Zhu S, Wurdak H, Wang Y, Galkin A, Tao H, Li J, Lyssiotis CA, Yan F, Tu BP, Miraglia L, Walker J, Sun F, Orth A, Schulz PG, Wu X. A genomic screen identifies TYRO3 as a MITF regulator in melanoma. Proc Natl Acad Sci USA. 2009;106(40):17025-17030.

    Not in our library10.1073/pnas.0909292106

  56. 56.

    Huber WE, Price ER, Widlund HR, Du J, Davies IJ, Wegner M, Fisher DE. A tissue-restricted cAMP transcriptional response: sOX10 modulates alpha-melanocyte-stimulating hormone-triggered expression of microphthalmia-associated transcription factor in melanocytes. J Biol Chem. 2003;278(46):45224-45230.

    Not in our library10.1074/jbc.m309036200

  57. 57.

    Saha B, Singh SK, Sarkar C, Bera R, Ratha J, Tobin DJ, Bhadra R. Activation of the Mitf promoter by lipid-stimulated activation of p38-stress signaling to CREB. Pigment Cell Res. 2006;19(6):595-605.

    Not in our library10.1111/j.1600-0749.2006.00348.x

  58. 58.

    Sakamoto KM, Frank DA. CREB in the pathophysiology of cancer: implications for targeting transcription factors for cancer therapy. Clin Cancer Res. 2009;15(8):2583-2587.

    Not in our library10.1158/1078-0432.ccr-08-1137

  59. 59.

    Sestakova B, Ondrusova L, Vachtenheim J. Cell cycle inhibitor p21/WAF1/CIP1 as a cofactor of MITF expression in melanoma cells. Pigment Cell Melanoma Res. 2010;23(2):238-251.

    Not in our library10.1111/j.1755-148x.2010.00670.x

  60. 60.

    Saito H, Yasumoto KI, Takeda K, Takahashi K, Fukuzaki A, Orikasa S, Shibahara S. Melanocyte-specific microphthalmia-associated transcription factor isoform activates its own gene promoter through physical interaction with lymphoid-enhancing factor 1. J Biol Chem. 2002;277(32):28787-28794.

    Not in our library10.1074/jbc.m203719200

  61. 61.

    Bellei B, Pitisci A, Catricala C, Larue L, Picardo M. Wnt/beta-catenin signaling is stimulated by alpha-melanocyte-stimulating hormone in melanoma and melanocyte cells: implication in cell differentiation. Pigment Cell Melanoma Res. 2010;24(2):309-325.

    Not in our library10.1111/j.1755-148x.2010.00800.x

  62. 62.

    Tatari MN, De Craene B, Soen B, Taminau J, Vermassen P, Goossens S, Haigh K, Cazzola S, Lambert J, Huylebroeck D, Haigh JJ, Berx G. ZEB2-transgene expression in the epidermis compromises the integrity of the epidermal barrier through the repression of different tight junction proteins. Cell Mol Life Sci. 2014;71(18):3599-3609.

    Not in our library10.1007/s00018-014-1589-0

  63. 63.

    Gheldof A, Hulpiau P, van Roy F, De Craene B, Berx G. Evolutionary functional analysis and molecular regulation of the ZEB transcription factors. Cell Mol Life Sci. 2012;69(15):2527-2541.

    Not in our library10.1007/s00018-012-0935-3

  64. 64.

    Sanchez-Tillo E, Liu Y, de Barrios O, Siles L, Fanlo L, Cuatrecasas M, Darling DS, Dean DC, Castells A, Postigo A. EMT-activating transcription factors in cancer: beyond EMT and tumor invasiveness. Cell Mol Life Sci. 2012;69(20):3429-3456.

    Not in our library10.1007/s00018-012-1122-2

  65. 65.

    Denecker G, Vandamme N, Akay O, Koludrovic D, Taminau J, Lemeire K, Gheldof A, De Craene B, Van Gele M, Brochez L, Udupi GM, Rafferty M, Balint B, Gallagher WM, Ghanem G, Huylebroeck D, Haigh J, van den Oord J, Larue L, Davidson I, Marine JC, Berx G. Identification of a ZEB2-MITF-ZEB1 transcriptional network that controls melanogenesis and melanoma progression. Cell Death Differ. 2014;21(8):1250-1261.

    Not in our library10.1038/cdd.2014.44

  66. 66.

    Liu Y, Ye F, Li Q, Tamiya S, Darling DS, Kaplan HJ, Dean DC. Zeb1 represses Mitf and regulates pigment synthesis, cell proliferation, and epithelial morphology. Invest Ophthalmol Vis Sci. 2009;50(11):5080-5088.

    Not in our library10.1167/iovs.08-2911

  67. 67.

    Vachtenheim J, Ondrusova L, Borovansky J. SWI/SNF chromatin remodeling complex is critical for the expression of microphthalmia-associated transcription factor in melanoma cells. Biochem Biophys Res Commun. 2010;392(3):454-459.

    Not in our library10.1016/j.bbrc.2010.01.048

  68. 68.

    Pierrat MJ, Marsaud V, Mauviel A, Javelaud D. Expression of microphthalmia-associated transcription factor (MITF), which is critical for melanoma progression, is inhibited by both transcription factor GLI2 and transforming growth factor β. J Biol Chem. 2012;287(22):17996-18004.

    Not in our library10.1074/jbc.m112.358341

  69. 69.

    Yang G, Li Y, Nishimura EK, Xin H, Zhou A, Guo Y, Dong L, Denning MF, Nickoloff BJ, Cui R. Inhibition of PAX3 by TGF-beta modulates melanocyte viability. Mol Cell. 2008;32(4):554-563.

    Not in our library10.1016/j.molcel.2008.11.002

  70. 70.

    He S, Li CG, Slobbe L, Glover A, Marshall E, Baguley BC, Eccles MR. PAX3 knockdown in metastatic melanoma cell lines does not reduce MITF expression. Melanoma Res. 2011;21(1):24-34.

    Not in our library10.1097/cmr.0b013e328341c7e0

  71. 71.

    Bonvin E, Falletta P, Shaw H, Delmas V, Goding CR. A phosphatidylinositol 3-kinase-PAX3 axis regulates Brn-2 expression in melanoma. Mol Cell Biol. 2012;32(22):4674-4683.

    Not in our library10.1128/mcb.01067-12

  72. 72.

    Liu F, Cao J, Wu J, Sullivan K, Shen J, Ryu B, Xu Z, Wei W, Cui R. Stat3-targeted therapies overcome the acquired resistance to vemurafenib in melanomas. J Invest Dermatol. 2013;133(8):2041-2049.

    Not in our library10.1038/jid.2013.32

  73. 73.

    Goodall J, Carreira S, Denat L, Kobi D, Davidson I, Nuciforo P, Sturm RA, Larue L, Goding CR. Brn-2 represses microphthalmia-associated transcription factor expression and marks a distinct subpopulation of microphthalmia-associated transcription factor-negative melanoma cells. Cancer Res. 2008;68(19):7788-7794.

    Not in our library10.1158/0008-5472.can-08-1053

  74. 74.

    Boyle GM, Woods SL, Bonazzi VF, Stark MS, Hacker E, Aoude LG, Dutton-Regester K, Cook AL, Sturm RA, Hayward NK. Melanoma cell invasiveness is regulated by miR-211 suppression of the BRN2 transcription factor. Pigment Cell Melanoma Res. 2011;24(3):525-537.

    Not in our library10.1111/j.1755-148x.2011.00849.x

  75. 75.

    Feige E, Yokoyama S, Levy C, Khaled M, Igras V, Lin RJ, Lee S, Widlund HR, Granter SR, Kung AL, Fisher DE. Hypoxia-mediated transcriptional repression of the melanoma-associated oncogene MITF. Proc Natl Acad Sci USA. 2011;108(43):E924-E933.

    Not in our library10.1073/pnas.1106351108

  76. 76.

    Busca R, Berra E, Gaggioli C, Khaled M, Bille K, Marchetti B, Thyss R, Fitsialos G, Larribere L, Bertolotto C, Virolle T, Barbry P, Pouyssegur J, Ponzio G, Ballotti R. Hypoxia-inducible factor 1α is a new target of microphthalmia-associated transcription factor (MITF) in melanoma cells. J Cell Biol. 2005;170(1):49-59.

    Not in our library10.1083/jcb.200501067

  77. 77.
    Expression and function of hypoxia inducible factor-1 alpha in human melanoma under non-hypoxic conditions · 2009
    Not checked
  78. 78.

    Hwang I, Park JH, Park HS, Choi KA, Seol KC, Oh SI, Kang S, Hong S. Neural stem cells inhibit melanin production by activation of Wnt inhibitors. J Dermatol Sci. 2013;72(3):274-283.

    Not in our library10.1016/j.jdermsci.2013.08.006

  79. 79.
    Gene expression profiling identifies microphthalmia-associated transcription factor (MITF) and Dickkopf-1 (DKK1) as regulators of microenvironment-driven alterations in melanoma phenotype. · 2014
    Not checked
  80. 80.

    Shah M, Bhoumik A, Goel V, Dewing A, Breitwieser W, Kluger H, Krajewski S, Krajewska M, Dehart J, Lau E, Kallenberg DM, Jeong H, Eroshkin A, Bennett DC, Chin L, Bosenberg M, Jones N, Ronai ZA. A role for ATF2 in regulating MITF and melanoma development. PLoS Genet. 2010;6(12):e1001258.

    Not in our library10.1371/journal.pgen.1001258

  81. 81.

    Anghel SI, Correa-Rochal R, Budinska E, Boligan KF, Abraham S, Colombetti S, Fontao L, Mariotti A, Rimoldi D, Ghanem GE, Fisher DE, Levy F, Delorenzi M, Piguet V. Breast cancer suppressor candidate-1 (BCSC-1) is a melanoma tumor suppressor that down regulates MITF. Pigment Cell Melanoma Res. 2012;25(4):482-487.

    Not in our library10.1111/j.1755-148x.2012.01018.x

  82. 82.

    Son J, Kim M, Jou I, Park KC, Kang HY. IFN-γ inhibits basal and α-MSH-induced melanogenesis. Pigment Cell Melanoma Res. 2014;27(2):201-208.

    Not in our library10.1111/pcmr.12190

  83. 83.

    Craig EA, Spiegelman VS. Inhibition of coding region determinant binding protein sensitizes melanoma cells to chemotherapeutic agents. Pigment Cell Melanoma Res. 2011;25(1):83-87.

    Not in our library10.1111/j.1755-148x.2011.00921.x

  84. 84.

    Bemis LT, Chen R, Amato CM, Classen EH, Robinson SE, Coffey DG, Erickson PF, Shellman YG, Robinson WA. MicroRNA-137 targets microphthalmia-associated transcription factor in melanoma cell lines. Cancer Res. 2008;68(5):1362-1368.

    Not in our library10.1158/0008-5472.can-07-2912

  85. 85.

    Luo C, Tetteh PW, Merz PR, Dickes E, Abukiwan A, Hotz-Wagenblatt A, Holland-Cunz S, Sinnberg T, Schittek B, Schadendorf D, Diederichs S, Eichmuller SB. miR-137 inhibits the invasion of melanoma cells through downregulation of multiple oncogenic target genes. J Invest Dermatol. 2013;133(3):768-775.

    Not in our library10.1038/jid.2012.357

  86. 86.

    Segura MF, Hanniford D, Menendez S, Reavie L, Zou X, Alvarez-Diaz S, Zakrzewski J, Blochin E, Rose A, Bogunovic D, Polsky D, Wei J, Lee P, Belitskaya-Levy I, Bhardwaj N, Osman I, Hernando E. Aberrant miR-182 expression promotes melanoma metastasis by repressing FOXO3 and microphthalmia-associated transcription factor. Proc Natl Acad Sci USA. 2009;106(6):1814-1819.

    Not in our library10.1073/pnas.0808263106

  87. 87.

    Yan D, Dong XD, Chen X, Yao S, Wang L, Wang J, Wang C, Hu DN, Qu J, Tu L. Role of microRNA-182 in posterior uveal melanoma: regulation of tumor development through MITF, BCL2 and cyclin D2. PLoS One. 2012;7(7):e40967.

    Not in our library10.1371/journal.pone.0040967

  88. 88.
    miR-148 regulates Mitf in melanoma cells. · 2010
    Not checked
  89. 89.

    Luo C, Merz PR, Chen Y, Dickes E, Pscherer A, Schadendorf D, Eichmuller SB. MiR-101 inhibits melanoma cell invasion and proliferation by targeting MITF and EZH2. Cancer Lett. 2013;341(2):240-247.

    Not in our library10.1016/j.canlet.2013.08.021

  90. 90.

    Guo J, Zhang JF, Wang WM, Cheung FW, Lu YF, Ng CF, Kung HF, Liu WK. MicroRNA-218 inhibits melanogenesis by directly suppressing microphthalmia-associated transcription factor expression. RNA Biol. 2014;11(6):732-741.

    Not in our library10.4161/rna.28865

  91. 91.

    Gajos-Michniewicz A, Duechler M, Czyz M. MiRNA in melanoma-derived exosomes. Cancer Lett. 2014;347(1):29-37.

    Not in our library10.1016/j.canlet.2014.02.004

  92. 92.

    Wu M, Hemesath TJ, Takemoto CM, Horstmann WA, Wells AG, Price ER, Fisher DZ, Fisher DE. c-Kit triggers dual phosphorylations, which couple activation and degradation of the essential melanocyte factor Mi. Genes Dev. 2000;14(3):301-312.

    Not in our library

  93. 93.

    Takeda K, Takemoto C, Kobayashi I, Watanabe A, Nobukuni Y, Fisher DE, Tachibana M. Ser298 of MITF, a mutation site in Waardenburg syndrome type 2, is a phosphorylation site with functional significance. Hum Mol Genet. 2000;9(1):125-132.

    Not in our library10.1093/hmg/9.1.125

  94. 94.

    Terragni J, Nayak G, Banerjee S, Medrano JL, Graham JR, Brennan JF, Sepulveda S, Cooper GM. The E-box binding factors Max/Mnt, MITF, and USF1 act coordinately with FoxO to regulate expression of proapoptotic and cell cycle control genes by phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3 signaling. J Biol Chem. 2011;286(42):36215-36227.

    Not in our library10.1074/jbc.m111.246116

  95. 95.

    Mansky KC, Sankar U, Han J, Ostrowski MC. Microphthalmia transcription factor is a target of the p38 MAPK pathway in response to receptor activator of NF-kappa B ligand signaling. J Biol Chem. 2002;277(13):11077-11083.

    Not in our library10.1074/jbc.m111696200

  96. 96.

    Levy C, Khaled M, Fisher DE. MITF: master regulator of melanocyte development and melanoma oncogene. Trends Mol Med. 2006;12(9):406-414.

    Not in our library10.1016/j.molmed.2006.07.008

  97. 97.

    Levy C, Sonnenblick A, Razin E. Role played by microphthalmia transcription factor phosphorylation and its zip domain in its transcriptional inhibition by PIAS3. Mol Cell Biol. 2003;23(24):9073-9080.

    Not in our library10.1128/mcb.23.24.9073-9080.2003

  98. 98.

    Levy C, Lee YN, Nechushtan H, Schueler-Furman O, Sonnenblick A, Hacohen S, Razin E. Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3. Blood. 2006;107(7):2839-2845.

    Not in our library10.1182/blood-2005-08-3325

  99. 99.

    Xu W, Gong L, Haddad MM, Bischof O, Campisi J, Yeh ET, Medrano EE. Regulation of microphthalmia-associated transcription factor MITF protein levels by association with the ubiquitin-conjugating enzyme hUBC9. Exp Cell Res. 2000;255(2):135-143.

    Not in our library10.1006/excr.2000.4803

  100. 100.

    Liu F, Singh A, Yang Z, Garcia A, Kong Y, Meyskens FL. MiTF links Erk1/2 kinase and p21CIP1/WAF1 activation after UVC radiation in normal human melanocytes and melanoma cells. Mol Cancer. 2010;9:214.

    Not in our library10.1186/1476-4598-9-214

  101. 101.
    Oncogenic BRAF Regulates Melanoma Proliferation through the Lineage Specific Factor MITF · 2008
    No notice
  102. 102.

    Zhao X, Fiske B, Kawakami A, Li J, Fisher DE. Regulation of MITF stability by the USP13 deubiquitinase. Nat Commun. 2011;2:414.

    Not in our library10.1038/ncomms1421

  103. 103.

    Larribere L, Hilmi C, Khaled M, Gaggioli C, Bille K, Auberger P, Ortonne JP, Ballotti R, Bertolotto C. The cleavage of microphthalmia-associated transcription factor, MITF, by caspases plays an essential role in melanocyte and melanoma cell apoptosis. Genes Dev. 2005;19(17):1980-1985.

    Not in our library10.1101/gad.335905

  104. 104.

    Murakami H, Arnheiter H. Sumoylation modulates transcriptional activity of MITF in a promoter-specific manner. Pigment Cell Res. 2005;18(4):265-277.

    Not in our library10.1111/j.1600-0749.2005.00234.x

  105. 105.

    Miller AJ, Levy C, Davis IJ, Razin E, Fisher DE. Sumoylation of MITF and its related family members TFE3 and TFEB. J Biol Chem. 2005;280(1):146-155.

    Not in our library10.1074/jbc.m411757200

  106. 106.

    Wang F, Marshall CB, Ikura M. Transcriptional/epigenetic regulator CBP/p300 in tumorigenesis: structural and functional versatility in target recognition. Cell Mol Life Sci. 2013;70(21):3989-4008.

    Not in our library10.1007/s00018-012-1254-4

  107. 107.

    Keenen B, Qi H, Saladi SV, Yeung M, de la Serna IL. Heterogeneous SWI/SNF chromatin remodeling complexes promote expression of microphthalmia-associated transcription factor target genes in melanoma. Oncogene. 2010;29(1):81-92.

    Not in our library10.1038/onc.2009.304

  108. 108.
    MITF-independent pro-survival role of BRG1-containing SWI/SNF complex in melanoma cells. · 2013
    Not checked
  109. 109.

    Mascarenhas JB, Littlejohn EL, Wolsky RJ, Young KP, Nelson M, Salgia R, Lang D. PAX3 and SOX10 activate MET receptor expression in melanoma. Pigment Cell Melanoma Res. 2010;23(2):225-237.

    Not in our library10.1111/j.1755-148x.2010.00667.x

  110. 110.

    Schepsky A, Bruser K, Gunnarsson GJ, Goodall J, Hallsson JH, Goding CR, Steingrimsson E, Hecht A. The microphthalmia-associated transcription factor Mitf interacts with beta-catenin to determine target gene expression. Mol Cell Biol. 2006;26(23):8914-8927.

    Not in our library10.1128/mcb.02299-05

  111. 111.

    Genovese G, Ghosh P, Li H, Rettino A, Sioletic S, Cittadini A, Sgambato A. The tumor suppressor HINT1 regulates MITF and β-catenin transcriptional activity in melanoma cells. Cell Cycle. 2012;11(11):2206-2215.

    Not in our library10.4161/cc.20765

  112. 112.

    Wardwell-Ozgo J, Dogruluk T, Gifford A, Zhang Y, Heffernan TP, van Doorn R, Creighton CJ, Chin L, Scott KL. HOXA1 drives melanoma tumor growth and metastasis and elicits an invasion gene expression signature that prognosticates clinical outcome. Oncogene. 2014;33(8):1017-1026.

    Not in our library10.1038/onc.2013.30

  113. 113.

    Kholmanskikh O, van Baren N, Brasseur F, Ottaviani S, Vanacker J, Arts N, van der Bruggen P, Coulie P, De Plaen E. Interleukins 1α and 1β secreted by some melanoma cell lines strongly reduce expression of MITF-M and melanocyte differentiation antigens. Int J Cancer. 2010;127:1625-1636.

    Not in our library10.1002/ijc.25182

  114. 114.

    Konieczkowski DJ, Johannessen CM, Abudayyeh O, Kim JW, Cooper ZA, Piris A, Frederick DT, Barzily-Rokni M, Straussman R, Haq R, Fisher DE, Mesirov JP, Hahn WC, Flaherty KT, Wargo JA, Tamayo P, Garraway LA. A melanoma cell state distinction influences sensitivity to MAPK pathway inhibitors. Cancer Discov. 2014;4(7):816-827.

    Not in our library10.1158/2159-8290.cd-13-0424

  115. 115.

    Pouryazdanparast P, Brenner A, Haghighat Z, Guitart J, Rademaker A, Gerami P. The role of 8q24 copy number gains and C-MYC expression in amelanotic cutaneous melanoma. Mod Pathol. 2012;25(9):1221-1226.

    Not in our library10.1038/modpathol.2012.75

  116. 116.

    Jane-Valbuena J, Widlund HR, Perner S, Johnson LA, Dibner AC, Lin WM, Baker AC, Nazarian RM, Vijayendran KG, Sellers WR, Hahn WC, Duncan LM, Rubin MA, Fisher DE, Garraway LA. An oncogenic role for ETV1 in melanoma. Cancer Res. 2010;70(5):2075-2084.

    Not in our library10.1158/0008-5472.can-09-3092

  117. 117.

    Nicholas C, Yang J, Peters SB, Bill MA, Baiocchi RA, Yan F, Sif S, Tae S, Gaudio E, Wu X, Grever MR, Young GS, Lesinski GB. PRMT5 is upregulated in malignant and metastatic melanoma and regulates expression of MITF and p27Kip1. PLoS One. 2013;8(9):e74710.

    Not in our library10.1371/journal.pone.0074710

  118. 118.

    Lin DC, Xu L, Ding LW, Sharma A, Liu LZ, Yang H, Tan P, Vadgama J, Karlan BY, Lester J, Urban N, Schummer M, Doan N, Said JW, Sun H, Walsh M, Thomas CJ, Patel P, Yin D, Chan D, Koeffler HP. Genomic and functional characterizations of phosphodiesterase subtype 4D in human cancers. Proc Natl Acad Sci USA. 2013;110(15):6109-6114.

    Not in our library10.1073/pnas.1218206110

  119. 119.

    Perego M, Tortoreto M, Tragni G, Mariani L, Deho P, Carbone A, Santinami M, Patuzzo R, Mina PD, Villa A, Pratesi G, Cossa G, Perego P, Daidone MG, Alison MR, Parmiani G, Rivoltini L, Castelli C. Heterogenous phenotype of human melanoma cells with in vitro and in vivo features of tumor-initiating cells. J Invest Dermatol. 2010;130(7):1877-1886.

    Not in our library10.1038/jid.2010.69

  120. 120.

    Ramgolam K, Lauriol J, Lalou C, Lauden L, Michel L, de la Grange P, Khatib AM, Aoudjit F, Charron D, Alcaide-Loridan C, Al-Daccak R. Melanoma spheroids grown under neural crest cell conditions are highly plastic migratory/invasive tumor cells endowed with immunomodulator function. PLoS One. 2011;6(4):e18784.

    Not in our library10.1371/journal.pone.0018784

  121. 121.

    Sztiller-Sikorska M, Koprowska K, Jakubowska J, Zalesna I, Stasiak M, Duechler M, Czyz M. Sphere formation and capacity of melanoma cells is affected by the microenvironment. Melanoma Res. 2012;22(3):215-224.

    Not in our library10.1097/cmr.0b013e3283531317

  122. 122.

    Ghislin S, Deshayes F, Lauriol J, Middendorp S, Martins I, Al-Daccak R, Alcaide-Loridan C. Plasticity of melanoma cells induced by neural cell crest conditions and three-dimensional growth. Melanoma Res. 2012;22(3):184-194.

    Not in our library10.1097/cmr.0b013e328351e7c4

  123. 123.

    Ennen M, Keime C, Kobi D, Mengus G, Lipsker D, Thibault-Carpentier C, Davidson I. Single-cell expression signatures reveal melanoma cell heterogeneity. Oncogene. 2014.

    Not in our library10.1038/onc.2014.262

  124. 124.

    Somasundaram R, Villanueva J, Herlyn M. Intratumoral heterogeneity as a therapy resistance mechanism: role of melanoma subpopulations. Adv Pharmacol. 2012;65:335-359.

    Not in our library10.1016/b978-0-12-397927-8.00011-7

  125. 125.

    Flaherty KT, Hodi FS, Fisher DE. From genes to drugs: targeted strategies for melanoma. Nat Rev Cancer. 2012;12(5):349-361.

    Not in our library10.1038/nrc3218

  126. 126.

    Haq R, Fisher DE. Targeting melanoma by small molecules: challenges ahead. Pigment Cell Melanoma Res. 2013;26(4):464-469.

    Not in our library10.1111/pcmr.12109

  127. 127.
    Pathways and therapeutic targets in melanoma · 2014
    No notice
  128. 128.

    Sztiller-Sikorska M, Koprowska K, Majchrzak K, Hartman M, Czyz M. Natural compounds’ activity against cancer stem-like or fast-cycling melanoma cells. PLoS One. 2014;9(3):e90783.

    Not in our library10.1371/journal.pone.0090783

  129. 129.

    Syed DN, Afaq F, Maddodi N, Johnson JJ, Sarfaraz S, Ahmad A, Setaluri V, Mukhtar H. Inhibition of human melanoma cell growth by the dietary flavonoid fisetin is associated with disruption of Wnt/β-catenin signaling and decreased Mitf levels. J Invest Dermatol. 2011;131(6):1291-1299.

    Not in our library10.1038/jid.2011.6

  130. 130.

    Botton T, Puissant A, Cheli Y, Tomic T, Giuliano S, Fajas L, Deckert M, Ortonne JP, Bertolotto C, Tartare-Deckert S, Ballotti R, Rocchi S. Ciglitazone negatively regulates CXCL1 signaling through MITF to suppress melanoma growth. Cell Death Differ. 2011;18(1):109-121.

    Not in our library10.1038/cdd.2010.75

  131. 131.

    Villareal MO, Han J, Ikuta K, Isoda H. Mechanisms of Mitf inhibition and morphological differentiation effects of hirsein A on B16 melanoma cells revealed by DNA microarray. J Dermatol Sci. 2012;67(1):26-36.

    Not in our library10.1016/j.jdermsci.2012.04.005

  132. 132.

    Johannessen CM, Johnson LA, Piccioni F, Townes A, Frederick DT, Donahue MK, Narayan R, Flaherty KT, Wargo JA, Root DE, Garraway LA. A melanocyte lineage program confers resistance to MAP kinase pathway inhibition. Nature. 2013;504(7478):138-142.

    Not in our library10.1038/nature12688

  133. 133.

    Chen G, Davies MA. Targeted therapy resistance mechanisms and therapeutic implications in melanoma. Hematol Oncol Clin N Am. 2014;28:523-536.

    Not in our library10.1016/j.hoc.2014.03.001

  134. 134.

    Roesch A. Tumor heterogeneity and plasticity as elusive drivers for resistance to MAPK pathway inhibition in melanoma. Oncogene. 2014.

    Not in our library10.1038/onc.2014.249

  135. 135.

    Smith MP, Ferguson J, Arozarena I, Hayward R, Marais R, Chapman A, Hurlstone A, Wellbrock C. Effect of SMURF2 targeting on susceptibility to MEK inhibitors in melanoma. J Natl Cancer Inst. 2013;105(1):33-46.

    Not in our library10.1093/jnci/djs471

  136. 136.

    Van Allen EM, Wagle N, Sucker A, Treacy DJ, Johannessen CM, Goetz EM, Place CS, Taylor-Weiner A, Whittaker S, Kryukov GV, Hodis E, Rosenberg M, McKenna A, Cibulskis K, Farlow D, Zimmer L, Hillen U, Gutzmer R, Goldinger SM, Ugurel S, Gogas HJ, Egberts F, Berking C, Trefzer U, Loquai C, Weide B, Hassel JC, Gabriel SB, Carter SL, Getz G, Garraway LA, Schadendorf D, Dermatologic Cooperative Oncology Group of Germany. The genetic landscape of clinical resistance to RAF inhibition in metastatic melanoma. Cancer Discov. 2014;4(1):94-109.

    Not in our library10.1158/2159-8290.cd-13-0617

  137. 137.

    Frederick DT, Piris A, Cogdill AP, Cooper ZA, Lezcano C, Ferrone CR, Mitra D, Boni A, Newton LP, Liu C, Peng W, Sullivan RJ, Lawrence DP, Hodi FS, Overwijk WW, Lizee G, Murphy GF, Hwu P, Flaherty KT, Fisher DE, Wargo JA. BRAF inhibition is associated with enhanced melanoma antigen expression and a more favorable tumor microenvironment in patients with metastatic melanoma. Clin Cancer Res. 2013;19(5):1225-1231.

    Not in our library10.1158/1078-0432.ccr-12-1630

  138. 138.

    Yokoyama S, Feige E, Poling LL, Levy C, Widlund HR, Khaled M, Kung AL, Fisher DE. Pharmacological suppression of MITF expression via HDAC inhibitors in the melanocyte lineage. Pigment Cell Melanoma Res. 2008;21(4):457-463.

    Not in our library10.1111/j.1755-148x.2008.00480.x

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