Structure and function of the membrane deformation AAA ATPase Vps4

Biochim Biophys Acta. 2012 Jan;1823(1):172-81. doi: 10.1016/j.bbamcr.2011.08.017. Epub 2011 Sep 8.

Abstract

The ATPase Vps4 belongs to the type-I AAA family of proteins. Vps4 functions together with a group of proteins referred to as ESCRTs in membrane deformation and fission events. These cellular functions include vesicle formation at the endosome, cytokinesis and viral budding. The highly dynamic quaternary structure of Vps4 and its interactions with a network of regulators and co-factors has made the analysis of this ATPase challenging. Nevertheless, recent advances in the understanding of the cell biology of Vps4 together with structural information and in vitro studies are guiding mechanistic models of this ATPase.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Animals
  • Endosomal Sorting Complexes Required for Transport / chemistry*
  • Endosomal Sorting Complexes Required for Transport / metabolism
  • Humans
  • Multivesicular Bodies / enzymology
  • Multivesicular Bodies / metabolism
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Transport
  • Vacuolar Proton-Translocating ATPases / chemistry*
  • Vacuolar Proton-Translocating ATPases / metabolism
  • Virus Release

Substances

  • Endosomal Sorting Complexes Required for Transport
  • Vacuolar Proton-Translocating ATPases
  • ATPases Associated with Diverse Cellular Activities
  • VPS4A protein, human