Modulation of Tight Junction Structure and Function by Kinases and Phosphatases Targeting Occludin

Abstract

Tight junctions (TJs) typically represent the most apical contacts in epithelial and endothelial cell layers where they play an essential role in the separation of extracellular or luminal spaces from underlying tissues in the body. Depending on the protein composition, TJs define the barrier characteristics and in addition maintain cell polarity. Two major families of integral membrane proteins form the typical TJ strand network, the tight junction-associated MARVEL protein (TAMP) family members occludin, tricellulin, and MarvelD3 as well as a specific set of claudins. Occludin was the first identified member of these tetraspanins and is now widely accepted as a regulator of TJ assembly and function. Therefore, occludin itself has to be tightly regulated. Phosphorylation of occludin appears to be of central importance in this context. Here we want to summarize current knowledge on the kinases and phosphatases directly modifying occludin, and their role in the regulation of TJ structure, function, and dynamics.

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Cited by papers we hold 7

• DUSP3 regulates phosphorylation-mediated degradation of occludin and is required for maintaining epithelial tight junction · 2022
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• Structure, Function, and Regulation of the Blood-Brain Barrier Tight Junction in Central Nervous System Disorders · 2020
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• Blood-Brain Barrier Damage in Ischemic Stroke and Its Regulation by Endothelial Mechanotransduction · 2020
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• Signaling pathways induced by serine proteases to increase intestinal epithelial barrier function. · 2017
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• Breaking down the barriers: the gut microbiome, intestinal permeability and stress-related psychiatric disorders · 2015
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• Heat Stress Reduces Intestinal Barrier Integrity and Favors Intestinal Glucose Transport in Growing Pigs · 2013
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• Tight junctions at the blood brain barrier: physiological architecture and disease-associated dysregulation · 2012
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