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A more recent version of this article appeared on May 5, 2006
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M512615200v1
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Papers In Press, published online ahead of print March 6, 2006
J. Biol. Chem, 10.1074/jbc.M512615200
Submitted on November 28, 2005
Accepted on March 6, 2006

The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation

Paula E. Row, Ian A. Prior, John McCullough, Michael J. Clague, and Sylvie Urbé

Physiological Laboratory, University of Liverpool, Liverpool L69 3BX

Corresponding Author: urbe{at}liv.ac.uk

UBPY is a ubiquitin specific protease that can deubiquitinate monoubiquitinated receptor tyrosine kinases, as well as process K48- and K63-linked polyubiquitin to lower denomination forms in vitro. Catalytically inactive UBPY localises to endosomes, which accumulate ubiquitinated proteins. We have explored the sequelae of siRNA-mediated knockdown of UBPY. Global levels of ubiquitinated protein increase and ubiquitin accumulates on endosomes, although free ubiquitin levels are unchanged. UBPY depleted cells have more and larger multi-vesicular endosomal structures, that are frequently associated through extended contact areas, characterised by regularly spaced, electron dense, bridging profiles. Degradation of acutely stimulated receptor tyrosine kinases, EGFR and Met, is strongly inhibited in UBPY knockdown cells suggesting that UBPY function is essential for growth factor receptor down-regulation. In contrast, stability of the UBPY binding partner STAM is dramatically compromised in UBPY knockdown cells. The cellular functions of UBPY are complex but clearly distinct from those of the K63-ubiquitin specific protease, AMSH, with which it shares a binding site on the SH3 domain of STAM.


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