Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways

Biochim Biophys Acta. 2012 Jan;1823(1):138-44. doi: 10.1016/j.bbamcr.2011.07.011. Epub 2011 Jul 23.

Abstract

The AAA-ATPase Cdc48/p97 controls a large array of cellular functions including protein degradation, cell division, membrane fusion through its ability to interact with and control the fate of ubiquitylated proteins. More recently, Cdc48/p97 also appeared to be involved in autophagy, a catabolic cell response that has long been viewed as completely distinct from the Ubiquitine/Proteasome System. In particular, conjugation by ubiquitin or ubiquitin-like proteins as well as ubiquitin binding proteins such as Cdc48/p97 and its cofactors can target degradation by both catabolic pathways. This review will focus on the recently described functions of Cdc48/p97 in autophagosome biogenesis as well as selective autophagy.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Autophagy*
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Humans
  • Mitochondria / metabolism
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Structure, Tertiary
  • Ribosomes / metabolism
  • Ubiquitinated Proteins / metabolism*
  • Valosin Containing Protein

Substances

  • Cell Cycle Proteins
  • Ubiquitinated Proteins
  • Proteasome Endopeptidase Complex
  • Adenosine Triphosphatases
  • Valosin Containing Protein