Vesicle trafficking and cell surface membrane patchiness

Biophys J. 2001 Jul;81(1):196-203. doi: 10.1016/S0006-3495(01)75691-3.

Abstract

Membrane proteins and lipids often appear to be distributed in patches on the cell surface. These patches are often assumed to be membrane domains, arising from specific molecular associations. However, a computer simulation (Gheber and Edidin, 1999) shows that membrane patchiness may result from a combination of vesicle trafficking and dynamic barriers to lateral mobility. The simulation predicts that the steady-state patches of proteins and lipids seen on the cell surface will decay if vesicle trafficking is inhibited. To test this prediction, we compared the apparent sizes and intensities of patches of class I HLA molecules, integral membrane proteins, before and after inhibiting endocytic vesicle traffic from the cell surface, either by incubation in hypertonic medium or by expression of a dominant-negative mutant dynamin. As predicted by the simulation, the apparent sizes of HLA patches increased, whereas their intensities decreased after endocytosis and vesicle trafficking were inhibited.

Publication types

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

MeSH terms

  • Biological Transport / drug effects
  • Cell Membrane / chemistry*
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism*
  • Clathrin / metabolism
  • Computer Simulation
  • Cytoplasmic Vesicles / drug effects
  • Cytoplasmic Vesicles / metabolism*
  • Dynamins
  • Endocytosis / drug effects
  • Fibroblasts
  • Fluorescence
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism
  • HLA-A Antigens / metabolism
  • HeLa Cells
  • Humans
  • Hypertonic Solutions / pharmacology
  • Membrane Lipids / metabolism
  • Membrane Microdomains* / drug effects
  • Membrane Proteins / metabolism
  • Microspheres
  • Models, Biological
  • Mutation
  • Temperature
  • Time Factors

Substances

  • Clathrin
  • HLA-A Antigens
  • Hypertonic Solutions
  • Membrane Lipids
  • Membrane Proteins
  • GTP Phosphohydrolases
  • Dynamins