Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast

Mol Biol Cell. 2018 Apr 15;29(8):948-963. doi: 10.1091/mbc.E17-11-0652. Epub 2018 Mar 30.

Abstract

Cdc48/p97 and the ubiquilin family of UBA-UBL proteins are known for their role in the retrotranslocation of damaged proteins from the endoplasmic reticulum. We demonstrate that Cdc48 and the ubiquilin-like proteins in yeast also play a role in the anterograde trafficking of proteins, in this case the vacuolar protease, Cps1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy
  • Carboxypeptidases / genetics
  • Carboxypeptidases / metabolism
  • Cell Cycle Proteins / metabolism
  • Endoplasmic Reticulum / metabolism
  • Multivesicular Bodies / metabolism
  • Nuclear Proteins / metabolism
  • Nucleocytoplasmic Transport Proteins / genetics
  • Nucleocytoplasmic Transport Proteins / metabolism
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Transport
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Ubiquitin / metabolism*
  • Valosin Containing Protein / genetics
  • Valosin Containing Protein / metabolism*
  • Vesicular Transport Proteins / genetics
  • Vesicular Transport Proteins / metabolism

Substances

  • Cell Cycle Proteins
  • DDI1 protein, S cerevisiae
  • NPL4 protein, S cerevisiae
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • UFD1 protein, S cerevisiae
  • Ubiquitin
  • Vesicular Transport Proteins
  • Carboxypeptidases
  • CPS1 protein, S cerevisiae
  • Proteasome Endopeptidase Complex
  • CDC48 protein, S cerevisiae
  • Valosin Containing Protein