Protein degradation: recognition of ubiquitinylated substrates

Curr Biol. 2004 Sep 21;14(18):R754-6. doi: 10.1016/j.cub.2004.09.012.

Abstract

A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.

Publication types

  • Review

MeSH terms

  • Carrier Proteins / metabolism
  • Cell Cycle Proteins / metabolism
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • DNA-Binding Proteins / metabolism
  • Models, Biological
  • Proteasome Endopeptidase Complex / physiology*
  • Protein Binding
  • Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Schizosaccharomyces pombe Proteins / metabolism
  • Ubiquitins / metabolism*
  • Ubiquitins / physiology*
  • Yeasts

Substances

  • Carrier Proteins
  • Cell Cycle Proteins
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • DNA-Binding Proteins
  • DSK2 protein, S cerevisiae
  • Proteins
  • RHP23 protein, S pombe
  • RPN10 protein, S cerevisiae
  • SIC1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • Ubiquitins
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease