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A more recent version of this article appeared on February 1, 2004
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Submitted on July 4, 2003
Revised on October 9, 2003
Accepted on October 28, 2003
1 Department of Cellular and Molecular Medicine; Howard Hughes Medical Institute; University of California, San Diego; School of Medicine; La Jolla, CA 92093-0668, These authors contributed equally to this work
2 Department of Cellular and Molecular Medicine; Howard Hughes Medical Institute; University of California, San Diego; School of Medicine; La Jolla, CA 92093-0668
* Corresponding author. E-mail address: semr{at}ucsd.edu.
The Multivesicular Body (MVB) Sorting pathway provides a mechanism for delivering transmembrane proteins into the lumen of the lysosome/vacuole. Recent studies demonstrated that ubiquitin modification acts in cis as a signal for the sorting of cargoes into this pathway. Here, we present results from a genetic selection designed to identify mutants that missort MVB cargoes. This selection identified a point mutation in ubiquitin ligase Rsp5 (Rsp5-326). At the permissive temperature, this mutant is specifically defective for ubiquitination and sorting of the ubiquitin-dependent MVB cargo pCPS (precursor Carboxypeptidase S) but not ligand-induced ubiquitination of Ste2. A previous study implicated Tul1 as the ubiquitin ligase responsible for MVB sorting of pCPS. However, we detected no defect in either the sorting or ubiquitination of pCPS in tul1 mutants. We had previously shown that Fab1 PI(3)P 5-kinase is also required for MVB sorting of pCPS, but not Ste2. However, our analyses reveal that fab1 mutants do not exhibit a defect in ubiquitination of pCPS. Thus both Rsp5 and Fab1 play distinct and essential roles in the targeting of biosynthetic MVB cargoes. However, while Rsp5 appears to be responsible for cargo ubiquitination, the precise role for Fab1 remains to be elucidated.
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