Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates

doi:10.1083/jcb.200112080

Published online 26 March 2002. doi:10.1083/jcb.200112080

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© The Rockefeller University Press, 0021-9525/2002/4/91 $5.00
The Journal of Cell Biology, Volume 157, Number 1, April 1, 2002 91-102

Article

Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein–ubiquitin conjugates

Naomi Bishop, Alistair Horman and Philip Woodman

School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom

Address correspondence to Philip Woodman, University of Manchester, Oxford Rd., Manchester M13 9PT, UK. Tel.: 44-161-275-7846. Fax: 44-161-275-5082. E-mail: pwoodman{at}fs1.scg.man.ac.uk

There is increasing evidence that ubiquitination of receptorsprovides an important endosomal sorting signal. Here we reportthat mammalian class E vacuolar protein-sorting (vps) proteinsrecognize ubiquitin. Both tumor susceptibility gene 101 (TSG101)/humanVPS (hVPS)28 and hepatocyte growth factor receptor substrate(Hrs) cytosolic complexes bind ubiquitin-agarose. TSG101 andhVPS28 are localized to endosomes that contain internalizedEGF receptor and label strongly for ubiquitinated proteins.Microinjection of anti-hVPS28 specifically retards EGF degradationand leads to endosomal accumulation of ubiquitin–proteinconjugates. Likewise, depletion of TSG101 impairs EGF traffickingand causes dramatic relocalization of ubiquitin to endocyticcompartments. Similar defects are found in cells overexpressingHrs, further emphasizing the links between class E protein function,receptor trafficking, and endosomal ubiquitination.

Key Words: endocytosis; EGF receptor; down-regulation; ubiquitin; multivesicular

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