Structural organization of the tight junctions

Biochim Biophys Acta. 2008 Mar;1778(3):646-59. doi: 10.1016/j.bbamem.2007.08.004. Epub 2007 Aug 24.


Tight junctions are the most apical organelle of the apical junctional complex and are primarily involved in the regulation of paracellular permeability and membrane polarity. Extensive research in the past two decades has identified not only the individual molecules of the tight junctions but also their mutual interactions, which are the focus of the present review article. While a complete map of the interactions among the tight junction molecules is probably far from being complete, the available evidence already allows outlining the general molecular architecture of the tight junctions. Here, with the aim of gaining deeper mechanistic understanding of tight junction assembly, regulation and function, we have subdivided the known molecular interactions into four major clusters that are centered on cell surface, polarity, cytoskeletal and signaling molecules.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / physiology
  • Cell Cycle
  • Cell Polarity
  • Cytoskeleton / physiology
  • Humans
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / physiology
  • Membrane Proteins / chemistry*
  • Membrane Proteins / physiology*
  • Models, Biological
  • Models, Molecular
  • Molecular Structure
  • Monomeric GTP-Binding Proteins / chemistry
  • Monomeric GTP-Binding Proteins / physiology
  • Multiprotein Complexes
  • Occludin
  • Signal Transduction
  • Tight Junctions / chemistry*
  • Tight Junctions / physiology*
  • Transcription Factors / physiology


  • Cell Adhesion Molecules
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Multiprotein Complexes
  • OCLN protein, human
  • Occludin
  • Transcription Factors
  • Monomeric GTP-Binding Proteins