BAR Domain Scaffolds in Dynamin-Mediated Membrane Fission

Cell. 2014 Feb 27;156(5):882-92. doi: 10.1016/j.cell.2014.02.017.

Abstract

Biological membranes undergo constant remodeling by membrane fission and fusion to change their shape and to exchange material between subcellular compartments. During clathrin-mediated endocytosis, the dynamic assembly and disassembly of protein scaffolds comprising members of the bin-amphiphysin-rvs (BAR) domain protein superfamily constrain the membrane into distinct shapes as the pathway progresses toward fission by the GTPase dynamin. In this Review, we discuss how BAR domain protein assembly and disassembly are controlled in space and time and which structural and biochemical features allow the tight regulation of their shape and function to enable dynamin-mediated membrane fission.

Publication types

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

MeSH terms

  • Animals
  • Cell Membrane / metabolism*
  • Clathrin-Coated Vesicles / metabolism
  • Dynamins / metabolism*
  • Endocytosis
  • Humans
  • Protein Structure, Tertiary

Substances

  • Dynamins