Cdc48/Shp1 participates in dissociation of protein complexes to regulate their activity

Curr Genet. 2021 Apr;67(2):263-265. doi: 10.1007/s00294-020-01136-1. Epub 2021 Jan 3.

Abstract

The AAA-ATPase p97/Cdc48 is one of the most abundant proteins in eukaryotes, and owing to its multiple functions, is considered the swiss army knife of cells. Recent findings demonstrate that p97/Cdc48 and its cofactor p47/Shp1 control the heavy metal stress response by active, signal-triggered disassembly of a multisubunit ubiquitin ligase. Here we review this pathway and describe recently achieved mechanistic insight into the role of p47/Shp1 in this process.

Keywords: Cadmium response; Cdc48/p97; SCF ubiquitin ligase; Shp1/p47.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / genetics
  • Cell Cycle Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / genetics*
  • Multiprotein Complexes / genetics*
  • Multiprotein Complexes / ultrastructure
  • Proteasome Endopeptidase Complex / genetics*
  • Proteasome Endopeptidase Complex / ultrastructure
  • Protein Binding / genetics
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / ultrastructure
  • Ubiquitin / genetics
  • Valosin Containing Protein / genetics*
  • Valosin Containing Protein / ultrastructure

Substances

  • Cell Cycle Proteins
  • Intracellular Signaling Peptides and Proteins
  • Multiprotein Complexes
  • SHP1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin
  • Adenosine Triphosphate
  • Proteasome Endopeptidase Complex
  • CDC48 protein, S cerevisiae
  • Valosin Containing Protein