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MBC in Press, published online ahead of print January 5, 2005
Mol. Biol. Cell 10.1091/mbc.E04-05-0425

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Submitted on May 21, 2004
Revised on December 10, 2004
Accepted on December 23, 2004

The Deubiquitinating Enzyme Ubp1 Affects Sorting of the ABC-Transporter Ste6 in the Endocytic Pathway

Carolin Schmitz,* Andrea Kinner,{dagger} and Ralf Kölling{ddagger}

Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany

Monitoring Editor: David Drubin

Deubiquitinating enzymes (Dubs) are potential regulators of ubiquitination-dependent processes. Here, we focus on a member of the yeast ubiquitin-specific processing protease (Ubp) familiy, the Ubp1 protein. We could show that Ubp1 exists in two forms: a longer membrane-anchored form (mUbp1) and a shorter soluble form (sUbp1) that appear to be independently expressed from the same gene. The membrane-associated mUbp1 variant could be localized to the endoplasmic reticulum (ER) membrane by sucrose-density-gradient centrifugation and by immunofluorescence microscopy. Overexpression of the soluble Ubp1 variant stabilizes the ABC-transporter Ste6, which is transported to the lysosome-like vacuole for degradation, and whose transport is regulated by ubiquitination. Ste6 stabilization was not the result of a general increase in deubiquitination activity, since overexpression of Ubp1 had no effect on the degradation of the ER-associated degradation (ERAD) substrate CPY* and most importantly on Ste6 ubiquitination itself. Also, overexpression of another yeast Dub, Ubp3, had no effect on Ste6 turnover. This suggests that the Ubp1 target is a component of the protein transport machinery. On Ubp1 overexpression, Ste6 accumulates at the cell surface, which is consistent with a role of Ubp1 at the internalization step of endocytosis or with enhanced recycling to the cell surface from an internal compartment.

Present addresses: *Institut für Pathologie, Heinrich-Heine-Universität Düsseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; {dagger}Max-Planck-Institut für Molekulare Physiologie, Postfach 500247, D-44202 Dortmund, Germany.

{ddagger}Corresponding author. E-mail: ralf.koelling{at}uni-duesseldorf.de






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