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Hsp60 Post-translational Modifications: Functional and Pathological Consequences

Celeste Caruso Bavisotto, Giusi Alberti, Alessandra Maria Vitale and 8 more (opens in a new tab)

Frontiers in Molecular Biosciences · 2020 · Review · CC BY

doi:10.3389/fmolb.2020.00095 (opens in a new tab)

Abstract

Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. The question is by what mechanism this protein can become multifaceted. Likely, one factor contributing to this diversity is post-translational modification (PTM). The amino acid sequence of Hsp60 contains many potential phosphorylation sites, and other PTMs are possible such as O-GlcNAcylation, nitration, acetylation, S-nitrosylation, citrullination, oxidation, and ubiquitination. The effect of some of these PTMs on Hsp60 functions have been examined, for instance phosphorylation has been implicated in sperm capacitation, docking of H2B and microtubule-associated proteins, mitochondrial dysfunction, tumor invasiveness, and delay or facilitation of apoptosis. Nitration was found to affect the stability of the mitochondrial permeability transition pore, to inhibit folding ability, and to perturb insulin secretion. Hyperacetylation was associated with mitochondrial failure; S-nitrosylation has an impact on mitochondrial stability and endothelial integrity; citrullination can be pro-apoptotic; oxidation has a role in the response to cellular injury and in cell migration; and ubiquitination regulates interaction with the ubiquitin-proteasome system. Future research ought to determine which PTM causes which variations in the Hsp60 molecular properties and functions, and which of them are pathogenic, causing chaperonopathies. This is an important topic considering the number of acquired Hsp60 chaperonopathies already catalogued, many of which are serious diseases without efficacious treatment.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 26, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

Post-translational modification (PTM) is a covalent change in an amino acid in a protein that can modify the properties and functions of the latter, for instance folding, ligand binding, migration to the place of residence, interaction with other molecules, and other specific roles, which in the case of molecular chaperones could be any of the various modes of chaperoning client polypeptides and any of their non-canonical tasks. The occurrence of a PTM depends on the spatial orientation of the target amino acid and on the neighboring residues in the protein molecule, which confer selectivity and reactivity of the former by affecting its electrophilic status.

Hsp60 is a molecular chaperone that belongs to the chaperonins of Group I; it is named HSPD1 or Cpn60 in humans and is classically described as a mitochondrial resident that maintains protein homeostasis in the organelle. However, this chaperonin plays various other roles in health and disease, particularly as a pathogenic factor in a range of inherited and acquired chaperonopathies. For these reasons, interest in Hsp60 has been steadily increasing in recent years, especially because it holds promise for developing new diagnostic and therapeutic procedures pertinent to common and serious chaperonopathies such as various types of cancer, and inflammatory and autoimmune disorders as well as for a range of neurodegenerative diseases. For example, Hsp60 inhibitors and modulators are being actively evaluated as novel anti-cancer agents.

Hsp60 occurs not only inside mitochondria but also in other intracellular locations, for example the cytosol, and extracellularly, and its functions vary accordingly, depending on the interactors that surround it at the various locations. For example, inside mitochondria Hsp60 assists the folding and trafficking of other proteins, but in the cytosol it can favor apoptosis or the contrary, for example in some cancer cells, and can thus be anti- or pro-cancer, respectively.

Structurally, the Hsp60 molecule has functional modules and three structural domains and if any of these modules-domains is altered by a PTM, its functions may be seriously impaired as shown, for example, with the chaperonin CCT. This type of modification might change Hsp60 from cytoprotective into pathogenic, causing a chaperonopathy. To the best of our knowledge, there is no article describing all known Hsp60 PTMs together, in a way that would be a useful resource for practitioners and scientists in their studies of Hsp60 chaperonopathies in patients or experimental models. The main goal of this article is to contribute to filling in this information gap. Consequently, we present a comprehensive review of known PTMs of Hsp60, with a brief discussion of the possible impact of a few of them on some of its properties and functions.

Hsp60 Structure and Chaperoning Cycle

Hsp60 is highly conserved in evolution, from bacteria and archaea to complex plants and animals.

In mammals, Hsp60 and its co-chaperone Hsp10 are classically located inside mitochondria where they constitute the protein folding apparatus with a mechanism elucidated using the bacterial homologues GroEL and GroES, respectively (references in;; ). Hsp60 forms a stable tetradecameric double-ring complex in the absence of Hsp10 and nucleotide. The crystal structure of Hsp60 in complex with Hsp10 shows a symmetric double-ring, American football-like structure with extensive interring contacts and the symmetry of the Hsp60 subunits within each ring observed in the bacterial chaperonin is not preserved in the human counterpart. Moreover, the interring nucleotide asymmetry that characterizes the GroEL folding cycle is absent, because both Hsp60 rings are in the ADP-bound state. Hsp60 binds unfolded proteins catalyzing their folding in an ATP dependent manner. Hsp10 acts as a cap sitting on the outer border of the mouth of the heptameric ring, opening and closing the tetradecamer central cavity, regulating both the interactions of the Hsp60 monomers and ATP hydrolysis. Hsp60 monomers are formed of three structural domains named apical, intermediate and equatorial (Figures 1, 2): (i) the apical domain binds the substrate and the co-chaperone and it is implicated in ATP turnover; (ii) the intermediate domain connects the apical with the equatorial domain; and (iii) the equatorial domain facilitates interactions between the single subunits within a ring and between the two heptameric rings of the chaperonin. Electron microscopic analysis of the human Hsp60 showed that the Hsp60/Hsp10 complex goes through a more complicated functional cycle than that of the GroEl/GroES complex, and this increased complexity depends on distinctive structural features of Hsp60 and of the Hsp60/Hsp10 complex. Hsp60 can start as a single ring that enters the double-ring cycle by binding to another ring along with Hsp10 and ATP. After ATP hydrolysis, Hsp60 releases ADP and Hsp10, returns to the single-ring structure and enters the next ATP-dependent cycle. Previous research had shown that mitochondrial Hsp60 exists in solution in dynamic equilibrium as monomer, heptamer (single ring), and tetradecamer (double ring), depending on protein concentration, temperature, and presence of cofactors (ATP and Hsp10). Also, biophysical methods have highlighted the importance of protein-protein interactions underlying the formation of stable Hsp60 oligomeric complexes (heptamers and tetradecamers), in equilibrium with minor populations of monomers, in aqueous solutions.

Data from the GroEL crystal structure and from the alignment of Hsp60 sequences from a wide range species have revealed highly conserved sequence segments and residues. The study of the connections of the conserved residues inside Hsp60 tri-dimensional structure and of their chemical and physical properties can lead to an understanding of the possible disruptive effects of PTMs on the protein stability and functions. One of the most complete papers regarding this topic reported several conserved residues between GroEL and Hsp60. For example, 246-PLLIIAED-253 and 275-AVKAPGFGDRRK-286 are two conserved sequences of the apical domain containing five aliphatic residues and enriched in charged residues. The sequence 191-EGMQFDRGYISPY-203 between the intermediate and the apical domain contains several aromatic residues for substrate binding. As connection between the intermediate and the apical domains, the conserved segments 363-EKLQERLAKLAGGVAVIKVG-382 and 402-ATRAAVEEGIVPGGG-416 include charged residues at positions 275–286 and 363–382 and the glycine triplet at positions 402–416 represent the binding domain for ATP/ADP. The apical domain contains also highly conserved hydrophobic/aromatic residues that contribute to substrate and co-chaperone binding such as Y199, Y203, Y222, F204, Y226, L234, L237, L259, V263, and V264. Any alteration, such as a PTM of the corresponding Hsp60 residues involved in substrate binding may result in functional defects, probably leading to protein misfolding and aggregation, and causing a chaperonopathy. The equatorial domain contains residues essential for the functioning of the chaperonin at positions 52–60 and 85–95 implicated in the binding of ATP/ADP and Mg2+/K+ ions. Any alteration of these sites or blocking them with a chemical compound might inactivate Hsp60. Other sites crucial for the typical chaperoning process mediated by GroEL/GroES during polypeptide folding are in the apical domain and represent the contact positions for GroES binding (L234, L237, and N265); these hydrophobic residues, highly conserved between species and necessary for substrate binding, contact GroES at the conserved hydrophobic residues I25, I26, L27, and A31.

The formation and functioning of the Hsp60 tetradecamer depend on the inter-monomer and intra-ring connections. The interaction between equatorial domains of contiguous monomers involves the hydrophobic residues I6, L73, L513, T517, and V521 from one side and the residues V39, L40, I49, and I60 on the opposite surface. The connections are completed via the presence of opposite charged interactions between K4-E518 and E61-R36. The conserved hydrophobic residue V464 represent the interactions between rings. The residues K105, E461, and E467, the residues A108, A109, and S463 with the opposite charged residues E434 and D345 contribute to the salt bridge K105-E434 and to allosteric switch. All these data regarding the chemical and physical characteristics of the residues distributed along GroEL and by similarity along Hsp60 domains show that several residues are crucial for the correct assembling of the two-ringed machine. Analysis of the crystal structure of the complex Hsp60/Hsp10 revealed some differences in the interring contact points of Hsp60 compared to GroEL but no differences were mentioned for other conserved and functionally important residues. The symmetric key of A109 in GroEL is replaced with a salt bridge between K109 and E105 in Hsp60 and a new symmetric hydrophobic interaction is formed between two A10 as well as a new symmetric hydrogen bond is formed between two D11. Moreover, the salt bridge between E461 and R452 that is present in GroEL is replaced by a salt bridge between E462 and K449 in Hsp60.

PTM of these and other residues, will most likely cause a failure of tetradecamer formation, impairing Hsp60 chaperoning ability and causing disease, a chaperonopathy.

Hsp60 Post-Translational Modifications

Hsp60 is a multifaceted molecule with canonical and non-canonical functions in a variety of physiological and pathological processes depending among other factors on cellular localization, Table 1. Any of the Hsp60 function may be affected by PTMs. It is, therefore, necessary to survey some of the roles of Hsp60 to gain insights on where, when, and how a PTM can make a significant impact.

In humans, Hsp60 is encoded by a nuclear gene (HSPD1) on chromosome 2q33.1, and subsequently translated in the cytosol. The protein consists of 573 amino acids (Figure 2), including a mitochondrial import signal (MIS) at the N-terminus of 26 amino acids necessary for its import into mitochondria and, in addition, a series of G repeats at the C-terminus with unknown function. The mitochondrial import mechanism of Hsp60 is very complex involving the potential of mitochondrial membranes and other chaperones present in the matrix space (e.g., Hsp70) and in the cytosol. Intra-mitochondrial cleavage of the MIS generates the mature Hsp60 protein, with 547 amino acids and a molecular mass of about 60 kDa.

Proteins with PTM are involved in all fundamental cellular processes. For example, lysine modification of nuclear proteins play a crucial role in gene regulation, and modified proteins are critical to maintain protein homeostasis. Likewise, phosphorylation, S-nitrosylation, and acetylation of mitochondrial proteins occur to modulate their functions inside the organelle.

PTMs can drastically change the function of a protein, which makes the understanding of the networks in which the modified protein is involved very difficult. There is abundant information regarding the effects of PTMs on some molecular chaperones like Hsp70 and Hsp90, but comparatively little is known about Hsp60 PTMs. Given the key role of Hsp60 in the regulation of cellular homeostasis, the decoding of the different PTMs that affect it can represent a turning point in many areas of cellular research. Some PTMs occurring in a specific and sequential manner describe a sort of code, the interpretation of which could reveal much about the activity of molecular chaperones in cells.

Hsp60 PTMs have not been investigated extensively even though elucidation of the impact of modifications of this multifaceted molecule will most likely shed light on the various mechanisms underpinning the diverse roles and migration of the chaperonin. It is possible that PTMs would affect key Hsp60 properties and functions if the modifications occur at one or more of the various critical sites on the Hsp60 molecule, such as the ATP-binding and substrate binding sites, the sites involved in intra- and inter-ring contacts, and sites pertaining to networking and to migrating and taking residence in the different intra- and extra-cellular locations in which Hsp60 resides and works. In this section we discuss Hsp60 PTMs described in the literature and the effects of these modifications.

Phosphorylation

Among the various PTMs that can occur on Hsp60 (Table 2 and Figure 2), phosphorylation is involved in physiological and pathological processes. The amino acid sequence of Hsp60 contains a number of potential phosphorylation sites (K72-V73-T74, K130-I131-S132, K157-Q158-S159, K250-I251-S252, K396-L397-S398, and K469-R470-T471) and the potential impact of their modification is still unclear. Hsp60 can be tyrosine phosphorylated at Y227 and Y243 and Hsp60 tyrosine phosphorylation is required for its surface activation. Under physiological conditions, for instance during the sperm-zona recognition, Hsp60 tyrosine phosphorylation triggers conformational changes, contributing to the activation of the zona pellucida receptor complex on the surface of mammalian spermatozoa and, thus, leads to sperm capacitation. In an in vitro model of leukemia, the extra-mitochondrial form of Hsp60 localized in the plasma-cell membrane was found to interact with the histone 2B (H2B) and its phosphorylation regulated the docking of H2B by Hsp60. Differential phosphorylation patterns of Hsp60 have been observed in rat hepatomas, in which the phosphorylation regulates the functions of microtubule associated proteins. Phosphorylated Hsp60 was identified as a molecular mediator for α3β1 integrin activation in the adhesion of metastatic breast cancer cells to the lymph nodes and to bone osteoblasts. Many malignant cells require tyrosine phosphorylation of Hsp60 to escape immunosurveillance by NK and CD8 T cells. Hyperglycemia induces an increased phosphorylation pattern of Hsp60, which might be associated to mitochondrial dysfunction. In response to rotavirus infection, phosphorylation and the subsequent transient degradation of mitochondrial Hsp60 are associated with an escape mechanism by which the virus leads to a delay of the early apoptosis activation.

O-GlcNAcylation, N-Glycosylation, and Acetylation

The O-linked-b-N-acetylglucosamine modification (O-GlcNAcylation) of Hsp60 occurs at the serine and/or threonine residues, which is important for regulating a range of biological activities of Hsp60, including metabolism, signaling, and transcription. Under high glucose condition, also an aberrant O-GlcNAcylation occurs in Hsp60 of myoblasts that it is associated with its phosphorylation, creating a crosstalk related to mitochondrial metabolism. In pancreatic β-cells, the O-GlcNAcylation of Hsp60 inhibits its binding to Bax, which is a pro-apoptotic protein that becomes free to translocate to mitochondria and activate cell death.

In tumors, as well as in normal cells under stress, N-glycosylated Hsp60 is expressed on the cell surface or secreted extracellularly. The chaperonin has three potential N-linked glycosylation sites, N103, N230, and N426. On the surface of a tumor, N-glycosylated Hsp60 would be able to modulate the immune response within the tumor microenvironment.

Our group demonstrated that Hsp60 hyperacetylation, following anticancer treatment in human tumor cells, contributes to the death of these cells. The post-translational hyperacetylation of Hsp60 might affect its interaction with p53 and signal for Hsp60 degradation via the ubiquitin-proteasome system, thus leading to cellular senescence and tumor growth arrest.

Large-scale proteomic approaches showed numerous mitochondrial acetylated proteins; however, in most cases, their regulation by acetyltransferases and deacetylases remains unclear. Sirtuin3 (SIRT3) is an NAD+-dependent mitochondrial protein deacetylase that regulates enzymes in crucial metabolic pathways. SIRT3-dependent acetylation of the Hsp60 co-chaperone, Hsp10 (Lys-56 residue) is critical in the dynamic interaction between the Hsp60/Hsp10, affecting protein folding in the mitochondria. Lysine acetylation is key for the Hsp60/Hsp10 complex activity. Therefore, alteration of the acetylation levels in certain amino acids of Hsp60 can promote development of disease.

Nitration and S-Nitrosylation

Mitochondrial metabolism and integrity are ensured by the correct functioning of mitochondrial proteins, including their adequate response to stress. A particular PTM, related to nitration, i.e., S-guanylation, was identified in the Hsp60 C442, which is located near the ATP-binding site and can play a crucial role in its chaperoning activity and in the ability to oligomerize (; Figure 1). This modification may influence Hsp60 stability and the functioning of the mitochondrial chaperoning subsystem with regard to the opening of mitochondrial permeability transition pore. Nitric oxide (NO) induces S-nitrosylation of Hsp60 C237 (Figure 1), facilitating interactions with the proteins required to maintain mitochondrial DNA stability during experimental E. coli peritonitis in mice. Also, Hsp60 S-nitrosylation might mediate the beneficial effect of statins on endothelial integrity, but the mechanism remains to be explained. The positive effect of S-nitrosylation on proteins, included Hsp60, may be of significance in the regulation of energy production in mitochondria and, thereby, would play a role in cytoprotection, as investigated in cardiac injury in vivo models, in which a pathway involving the S-nitrosylation of key cardioprotective proteins was described. Along this line of thought, a role of GAPDH as mediator of NO transport in mitochondria has been proposed. Among the cysteine residues involved in S-nitrosylation, C442 and C237 are present in Hsp60 (Figure 1) but not in GroEL and represent interesting sites for the development of electrophilic Hsp60-binding compounds.

Hsp60 nitration, e.g., in response to an excess of ROS, was shown to decrease ATP-hydrolysis activity, which disrupts the interaction of the chaperonin with its substrates and, thus, inhibits its substrate-folding ability. These serious effects of nitration happen because the modification most probably occurs in the highly conserved residues Y222 and Y226 of the apical domain (Figure 1), and this domain is crucial for Hsp10 and substrate binding by Hsp60. In pancreatic β-cells, Hsp60 nitration on the ATP binding site affects the process by which the insulin is secreted in secretory granules. Therefore, this could be a mechanism underlying the onset and progression of diabetes.

Hsp60 nitration could be a signal to release it into the extracellular space and circulation, for example via exosomes, where it would interact with the immune system.

In mitochondria, NO has an ambiguous role. On the one hand, NO produces various inhibiting effects on electron transport, and prolonged exposure is pro-apoptotic. On the other hand, NO induces S-nitrosylation of Hsp60 C237 (Figure 1), facilitating interactions with the proteins required to maintain mitochondrial DNA stability during experimental E. coli peritonitis in mice. Also, Hsp60 S-nitrosylation could mediate the beneficial effect of statins on endothelial integrity, but the mechanism remains unclear.

Citrullination and Methylation

Hsp60 is also known to be subjected to citrullination or deamination, which is a conversion of the amino acid arginine into the amino acid citrulline. Citrullinated Hsp60 was found in the surface of cells of a human sarcoma osteogenic cell line, inducing apoptosis through TLR4 signaling, a mechanism involved in joint damage in patients with rheumatoid arthritis. Data from different cell lines demonstrated that one functional methylation present on Hsp60 is the mono-methylated lysine 490 (K490me1). Senescent fibroblasts showed low level of asymmetric arginine di-methylation of Hsp60 compared to low-passage fibroblasts. This means that arginine asymmetric di-methylation of Hsp60 is correlated with the proliferation potential of cells and might be useful as a marker of cellular senescence.

Oxidation and Biotinylation

As a redox sensitive protein, Hsp60 is oxidized in HepG2 cells exposed to alcohol and it is responsible for cellular injury and cell migration. The C-terminal motif in Hsp60 might be considered a ROS acceptor thanks to a combination of PTMs in its residues. It has been proposed that biotinylation of lysines in Hsp60 close proximity to sulfoxidation sites (methionine) contributes toward the elimination of ROS via the methionine/methionine sulfoxide reductase pathway in human cell cultures.

Ubiquitination

In monocytes treated with azacytidine, a stress response occurs with Hsp60 upregulation and ubiquitination in its K396 residue (; Figure 1). The role of this PTM is still unclear, but it may play important roles in key cellular processes, such as in the stress-activated ubiquitin-proteasome pathway. A mutation in the target point of the small ubiquitin-like modifier (SUMO) contributes to aberrant growth morphology in Candida albicans, confirming the importance of Hsp60 for cell survival under certain stress conditions.

Conclusion and Perspectives for the Future

PTMs of Hsp60 have effects on its properties and functions, for instance ATP and substrate binding, and interaction with the co-chaperonin Hsp10, all of which in turn very likely have an impact on the chaperoning ability and on any of the other roles played by this chaperonin. Sites that undergo PTM are distributed in all structural domains of Hsp60 and can affect any of its functional modules, suggesting that any one of the many functions, canonical and non-canonical, of this chaperonin may be affected by the modifications. Since Hsp60 is essential to the maintenance of cellular and tissue physiology, it is of great interest to elucidate which PTMs occur in health and in the various diseases, i.e., Hsp60 chaperonopathies, in which the chaperonin is known or suspected to play an etiopathogenic role. Likewise, it would be very useful to identify PTMs that control, or at least partly determine, the Hsp60 locale of residence inside and outside cells. The chaperonin may act intracellularly or at sites distant from its cell of origin, and the destination may be dictated by specific modifications. This emphasizes the need for more studies on Hsp60 PTMs, particularly in cancer and other serious diseases, in which spread of the disease may be associated with Hsp60 migration or with other aberrant properties of the chaperonin that make it pathogenic. Furthermore, learning about PTMs and their effects on the properties and functions of Hsp60 will reveal clues on what sites and modifications may be used to either block the chaperonin (negative chaperonotherapy in case Hsp60 is an etiopathogenic factor), or to boost its activity (positive chaperonotherapy in cases of chaperonopathies by defect). In this regard, the newly reported crystal structure of the Hsp60/Hsp10 complex will be instrumental to dissect the possible effects of PTMs on structure and function.

Author Contributions

AM, EC, FC, and AJM conceived the idea and performed the final editing and revision. CCB, GA, LP, and AM collected material, wrote, and revised the manuscript. AV prepared the figures. CC, FR, and MG reviewed the conclusions. All the authors read and approved the manuscript.

Conflict of Interest

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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