Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis

Trends Cell Biol. 2006 Oct;16(10):493-8. doi: 10.1016/j.tcb.2006.08.004. Epub 2006 Sep 1.


Endocytosis is an important way for cells to take up liquids and particles from their environment. It requires membrane bending to be coupled with membrane fission, and the actin cytoskeleton has an active role in membrane remodelling. Here, we review recent research into the function of Bin-Amphiphysin-Rvs (BAR) domain proteins, which can sense membrane curvature and recruit actin to membranes. BAR proteins interact with the endocytic and cytoskeletal machinery, including the GTPase dynamin (which mediates vesicle fission), N-WASP (an Arp2/3 complex regulator) and synaptojanin (a phosphoinositide phosphatase). We describe three classes of BAR domains, BAR, N-BAR and F-BAR, providing examples of each discussing and how they function in linking membranes to the actin cytoskeleton in endocytosis.

MeSH terms

  • Actins / physiology*
  • Animals
  • Carrier Proteins / physiology*
  • Cell Division / physiology
  • Cell Membrane / physiology*
  • Clathrin / physiology*
  • Coated Pits, Cell-Membrane / physiology
  • Cytoskeleton / physiology
  • Dynamins / metabolism
  • Endocytosis / physiology*
  • Humans
  • Membrane Lipids / physiology
  • Membrane Proteins / physiology*


  • Actins
  • Carrier Proteins
  • Clathrin
  • Membrane Lipids
  • Membrane Proteins
  • Dynamins