Golgi Reassembly After Mitosis: The AAA Family Meets the Ubiquitin Family

Biochim Biophys Acta. 2005 Jun 30;1744(2):108-19. doi: 10.1016/j.bbamcr.2005.03.011. Epub 2005 Apr 9.

Abstract

The Golgi apparatus in animal cells breaks down at the onset of mitosis and is later rebuilt in the two daughter cells. Two AAA ATPases, NSF and p97/VCP, have been implicated in regulating membrane fusion steps that lead to regrowth of Golgi cisternae from mitotic fragments. NSF dissociates complexes of SNARE proteins, thereby reactivating them to mediate membrane fusion. However, NSF has a second function in regulating SNARE pairing together with the ubiquitin-like protein GATE-16. p97/VCP, on the other hand, is involved in a cycle of ubiquitination and deubiquitination of an unknown target that governs Golgi membrane dynamics. Here, these findings are reviewed and discussed in the context of the increasingly evident role of ubiquitin in membrane traffic processes.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Catalysis
  • Cell Cycle Proteins / metabolism
  • Golgi Apparatus / metabolism*
  • Humans
  • Membrane Fusion
  • Mitosis / physiology*
  • Models, Biological
  • SNARE Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Ubiquitin / metabolism*
  • Valosin Containing Protein
  • Vesicular Transport Proteins / metabolism

Substances

  • Cell Cycle Proteins
  • SNARE Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Ubiquitin
  • Vesicular Transport Proteins
  • Adenosine Triphosphatases
  • VCP protein, human
  • Valosin Containing Protein