Membrane-protein interactions in cell signaling and membrane trafficking

Wonhwa Cho, Robert V. Stahelin

Research output: Contribution to journalReview article

402 Citations (Scopus)

Abstract

Research in the past decade has revealed that many cytosolic proteins are recruited to different cellular membranes to form protein-protein and lipid-protein interactions during cell signaling and membrane trafficking. Membrane recruitment of these peripheral proteins is mediated by a growing number of modular membrane-targeting domains, including C1, C2, PH, FYVE, PX, ENTH, ANTH, BAR, FERM, and tubby domains, that recognize specific lipid molecules in the membranes. Structural studies of these membrane-targeting domains demonstrate how they specifically recognize their cognate lipid ligands. However, the mechanisms by which these domains and their host proteins are recruited to and interact with various cell membranes are only beginning to unravel with recent computational studies, in vitro membrane binding studies using model membranes, and cellular translocation studies using fluorescent protein-tagged proteins. This review summarizes the recent progress in our understanding of how the kinetics and energetics of membrane-protein interactions are regulated during the cellular membrane targeting and activation of peripheral proteins.

Original languageEnglish (US)
Pages (from-to)119-151
Number of pages33
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume34
DOIs
StatePublished - Jun 30 2005

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Cell signaling
Cell membranes
Membrane Proteins
Cell Membrane
Proteins
Membranes
Lipids
Chemical activation
Ligands

Keywords

  • Kinetics and energetics
  • Lipid mediators
  • Membrane-targeting domains
  • Peripheral proteins
  • Phosphoinositides
  • Reversible membrane recruitment

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

Membrane-protein interactions in cell signaling and membrane trafficking. / Cho, Wonhwa; Stahelin, Robert V.

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 34, 30.06.2005, p. 119-151.

Research output: Contribution to journalReview article

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