Cell Biochemistry and Biophysics

, Volume 60, Issue 1, pp 39–46

Regulation of Endocytic Sorting by ESCRT–DUB-Mediated Deubiquitination

  • Michelle H. Wright
  • Ilana Berlin
  • Piers D. Nash
Original Paper

DOI: 10.1007/s12013-011-9181-9

Cite this article as:
Wright, M.H., Berlin, I. & Nash, P.D. Cell Biochem Biophys (2011) 60: 39. doi:10.1007/s12013-011-9181-9

Abstract

Endocytosis of cell surface receptors mediates cellular homeostasis by coordinating receptor distribution with downstream signal transduction and attenuation. Post-translational modification with ubiquitin of these receptors, as well as the proteins that comprise the endocytic machinery, modulates cargo progression along the endocytic pathway. The interplay between ubiquitination states of cargo and sorting proteins drives trafficking outcomes by directing endocytosed material toward either lysosomal degradation or recycling. Deubiquitination by specific proteinases creates a reversible system that promotes spatial and temporal organization of endosomal sorting complexes required for transport (ESCRTs) and supports regulated cargo trafficking. Two dubiquitinating enzymes—ubiquitin-specific protease 8 (USP8/Ubpy) and associated molecule with the SH3 domain of STAM (AMSH)—interact with ESCRT components to modulate the ubiquitination status of receptors and relevant sorting proteins. In doing so, these ESCRT–DUBs control receptor fate and sorting complex function through a variety of mechanisms described herein.

Keywords

Endocytosis Ubiquitin Receptor Protease Deubiquitylase 

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Michelle H. Wright
    • 1
  • Ilana Berlin
    • 1
  • Piers D. Nash
    • 1
    • 2
  1. 1.Ben May Department for Cancer ResearchThe University of ChicagoChicagoUSA
  2. 2.GCISChicagoUSA

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