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Tight Junction Structure and Function Revisited
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DOI：10.1016/j.tcb.2020.08.004.png)
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Abstract
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Tight junctions (TJs) are intercellular junctions critical for building the epithelial barrier and maintaining epithelial polarity. The claudin family of membrane proteins play central roles in TJ structure and function. However, recent findings have uncovered claudin-independent aspects of TJ structure and function, and additional players including junctional adhesion molecules (JAMs), membrane lipids, phase separation of the zonula occludens (ZO) family of scaffolding proteins, and mechanical force have been shown to play important roles in TJ structure and function. In this review, we discuss how these new findings have the potential to transform our understanding of TJ structure and function, and how the intricate network of TJ proteins and membrane lipids dynamically interact to drive TJ assembly.
Keywords:
PROTEIN-KINASE-C
ADHESION MOLECULE
OCCLUDIN PHOSPHORYLATION
JAM-A
POSSIBLE INVOLVEMENT
PHASE-SEPARATION
CLAUDIN STRANDS
ZONULA ADHERENS
DIRECT BINDING
ZO-1
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