Protein modules as organizers of membrane structure

Curr Opin Cell Biol. 1999 Aug;11(4):432-9. doi: 10.1016/S0955-0674(99)80062-3.


Investigations conducted over the past 18 months have shed new light on how modular protein-binding domains, in particular PDZ domains, co-ordinate the assembly of functional plasma membrane domains. Members of the MAGUK (membrane-associated guanylate kinase) protein family, like PSD-95, use multiple domains to cluster ion channels, receptors, adhesion molecules and cytosolic signaling proteins at synapses, cellular junctions, and polarized membrane domains. Other PDZ proteins, like the Drosophila protein INAD and the epithelial Na(+)/H(+) regulatory factor (NHERF), organize cellular signaling by localizing transmembrane and cytosolic components to specific membrane domains and assembling these components into functional complexes. The organization of these proteins into discreet structures has functional consequences for downstream signaling.

Publication types

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

MeSH terms

  • Animals
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism*
  • Drosophila
  • Drosophila Proteins*
  • Epithelial Cells / metabolism
  • Eye Proteins / metabolism
  • Humans
  • Intercellular Junctions / metabolism
  • Ion Channels
  • Membrane Proteins / metabolism*
  • Phosphoproteins / metabolism
  • Receptors, Cell Surface / metabolism
  • Signal Transduction
  • Sodium-Hydrogen Exchangers
  • Synapses / metabolism


  • Drosophila Proteins
  • Eye Proteins
  • Ion Channels
  • Membrane Proteins
  • Phosphoproteins
  • Receptors, Cell Surface
  • Sodium-Hydrogen Exchangers
  • inaD protein, Drosophila
  • sodium-hydrogen exchanger regulatory factor