Molecular architecture of tight junctions

Annu Rev Physiol. 1998;60:121-42. doi: 10.1146/annurev.physiol.60.1.121.

Abstract

The tight junction creates a regulated barrier in the paracellular pathway and, together with the actin-rich adherens junction, forms a functional unit called the apical junction complex. A growing number of tight junction-associated proteins have been identified, but functions are defined for only a few. The intercellular barrier is formed by rows of the transmembrane protein occludin, which is bound on the cytoplasmic surface to ZO-1 and ZO-2. These proteins are members of the membrane-associated guanylate kinase (MAGUK) protein family and are likely to have both structural and signaling roles. Junctional plaque proteins without known functions include cingulin, p130, and 7H6; single reports describe ZA-1TJ and symplekin. Many cellular signaling pathways affect assembly and sealing of junctions. Transducing proteins, which localize within the junction, include both heterotrimeric and rho-related GTP-binding proteins, PKC-zeta and nonreceptor tyrosine kinases. Control of perijunctional actin may be the unifying mechanism for regulating paracellular permeability.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Guanylate Kinases
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Nucleoside-Phosphate Kinase / metabolism
  • Signal Transduction / physiology
  • Tight Junctions / chemistry*
  • Tight Junctions / enzymology
  • Tight Junctions / physiology

Substances

  • Membrane Proteins
  • Nucleoside-Phosphate Kinase
  • Guanylate Kinases