Post-translational modifications of tight junction transmembrane proteins and their direct effect on barrier function

Biochim Biophys Acta Biomembr. 2020 Sep 1;1862(9):183330. doi: 10.1016/j.bbamem.2020.183330. Epub 2020 May 3.

Abstract

Post-translational modifications (PTMs) such as phosphorylation, ubiquitination or glycosylation are processes affecting the conformation, stability, localization and function of proteins. There is clear evidence that PTMs can act upon tight junction (TJ) proteins, thus modulating epithelial barrier function. Compared to transcriptional or translational regulation, PTMs are rapid and more dynamic processes so in the context of barrier maintenance they might be essential for coping with changing environmental or external impacts. The aim of this review is to extract literature deciphering PTMs in TJ proteins directly contributing to epithelial barrier changes in permeability to ions and macromolecules. It is not intended to cover the entire scope of PTMs in TJ proteins and should rather be understood as a digest of TJ protein modifications directly resulting in the tightening or opening of the epithelial barrier.

Keywords: Barrier function; Cell-cell contact; Claudin; Junctional adhesion molecule; LSR/angulin; Occludin; Permeability; Post-translational modification; Tight junction; Transepithelial resistance; Tricellulin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Epithelial Cells / chemistry
  • Humans
  • Intestinal Mucosa / chemistry
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Phosphorylation
  • Protein Processing, Post-Translational / genetics*
  • Protein Transport / genetics*
  • Tight Junction Proteins / genetics*
  • Tight Junctions / genetics*

Substances

  • Membrane Proteins
  • Tight Junction Proteins