Role of ubiquitination in endocytic trafficking of G-protein-coupled receptors

James N Hislop, Mark von Zastrow

Research output: Contribution to journalArticlepeer-review

81 Citations (Scopus)


Lysyl ubiquitination has long been known to target cytoplasmic proteins for proteasomal degradation, and there is now extensive evidence that ubiquitination functions in vacuolar/lysosomal targeting of membrane proteins from both the biosynthetic and endocytic pathways. G-protein-coupled receptors (GPCRs) represent the largest and most diverse family of membrane proteins, whose function is of fundamental importance both physiologically and therapeutically. In this review, we discuss the role of ubiquitination in the vacuolar/lysosomal downregulation of GPCRs through the endocytic pathway, with a primary focus on lysosomal trafficking in mammalian cells. We will summarize evidence indicating that mammalian GPCRs are regulated by ubiquitin-dependent mechanisms conserved in budding yeast, and then consider evidence for additional ubiquitin-dependent and -independent regulation that may be specific to animal cells.
Original languageEnglish
Pages (from-to)137-148
Number of pages12
Issue number2
Early online date15 Oct 2010
Publication statusPublished - Feb 2011

Bibliographical note

© 2010 John Wiley & Sons A/S.


  • animals
  • cell membrane
  • endocytosis
  • humans
  • membrane proteins
  • protein transport
  • receptors, G-protein-coupled
  • saccharomycetales
  • ubiquitin
  • ubiquitination


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