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Published online 15 May 2006. doi:10.1083/jcb.200602082
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 4, 463-468
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Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes

Susan M. Millard1,2,3 and Stephen A. Wood1,2

1 Child Health Research Institute, North Adelaide, South Australia 5006, Australia
2 School of Molecular and Biomedical Science and 3 Centre for the Molecular Genetics of Development, University of Adelaide, South Australia 5005, Australia

Correspondence to Stephen A. Wood: stephen.wood{at}adelaide.edu.au

Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light. However, a clear understanding of ubiquitin-dependent protein localization cannot be achieved without knowledge of the role of deubiquitylating enzymes (DUBs). DUBs, by definition, function downstream in ubiquitin pathways and, as such, have the potential to be the final editors of protein ubiquitylation status, thus determining substrate fate. This paper assimilates the current evidence concerning the substrates and activities of DUBs that regulate protein trafficking.

Abbreviations used in this paper: DUB, deubiquitylating enzyme; EGFR, EGF receptor; MVB, multivesicular body; STAM, signal-transducing adaptor molecule; UCH, ubiquitin COOH-terminal hydrolase; USP, ubiquitin-specific protease.


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