AAA+ ATPases: Achieving Diversity of Function With Conserved Machinery

Traffic. 2007 Dec;8(12):1657-67. doi: 10.1111/j.1600-0854.2007.00642.x. Epub 2007 Sep 26.

Abstract

AAA+ adenosine triphosphatases (ATPases) are molecular machines that perform a wide variety of cellular functions. For instance, they can act in vesicle transport, organelle assembly, membrane dynamics and protein unfolding. In most cases, the ATPase domains of these proteins assemble into active ring-shaped hexamers. As AAA+ proteins have a common structure, a central issue is determining how they use conserved mechanistic principles to accomplish specific biological actions. Here, we review the features and motifs that partially define AAA+ domains, describe the cellular activities mediated by selected AAA+ proteins and discuss the recent work, suggesting that various AAA+ machines with very different activities employ a common core mechanism. The importance of this mechanism to human health is demonstrated by the number of genetic diseases caused by mutant AAA+ proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Amino Acid Motifs
  • Animals
  • Binding Sites
  • Cell Membrane / metabolism
  • Conserved Sequence
  • Humans
  • Hydrolysis
  • Microtubules / chemistry
  • Models, Biological
  • Molecular Conformation
  • Mutation
  • Protein Conformation
  • Protein Denaturation
  • Protein Structure, Tertiary
  • Spastin

Substances

  • Adenosine Triphosphatases
  • Spastin
  • SPAST protein, human