Membrane transport: ubiquitylation in endosomal sorting

Curr Biol. 2001 Nov 13;11(22):R932-4. doi: 10.1016/s0960-9822(01)00558-9.

Abstract

In yeast, membrane proteins from the biosynthetic and endocytic pathways must be ubiquitylated for sorting to inward-budding vesicles in late endosomes, which give rise to multivesicular bodies. A conserved protein complex containing the yeast Vps23p or its mammalian counterpart Tsg101 may act as the ubiquitin receptor.

Publication types

  • Review

MeSH terms

  • Animals
  • Biological Transport
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • DNA-Binding Proteins / metabolism
  • Endosomal Sorting Complexes Required for Transport
  • Endosomes / metabolism*
  • Fungal Proteins / metabolism*
  • Humans
  • Protein Transport
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / metabolism
  • Ubiquitin / metabolism*
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Fungal Proteins
  • STP22 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Tsg101 protein
  • Ubiquitin
  • Vesicular Transport Proteins