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MBC in Press, published online ahead of print November 29, 2006
Mol. Biol. Cell 10.1091/mbc.E06-07-0588

A more recent version of this article appeared on February 1, 2007
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Submitted on July 10, 2006
Revised on October 26, 2006
Accepted on November 20, 2006

Efficient Cargo Sorting by ESCRT-I and the Subsequent Release of ESCRT-I from MVBs Requires the Subunit Mvb12

Matt Curtiss, Charles Jones, and Markus Babst

Department of Biology, University of Utah, Salt Lake City, UT 84112-9202

Monitoring Editor: Sandra Lemmon

The ESCRT-I protein complex functions in recognition and sorting of ubiquitinated transmembrane proteins into multivesicular body (MVB) vesicles. It has been shown that ESCRT-I contains the proteins Vps23, Vps28 and Vps37. We identified an additional subunit of yeast ESCRT-I called Mvb12 which seems to associate with ESCRT-I by binding to Vps37. Transient recruitment of ESCRT-I to MVBs results in the rapid degradation of Mvb12. In contrast to mutations in other ESCRT-I subunits which result in strong defects in MVB cargo sorting, deletion of MVB12 resulted in only a partial sorting phenotype. This trafficking defect was fully suppressed by overexpression of the ESCRT-II complex. Mutations in MVB12 did not affect recruitment of ESCRT-I to MVBs, but resulted in delivery of ESCRT-I to the vacuolar lumen via the MVB pathway. Together, these observations suggest that Mvb12 may function in regulating the interactions of ESCRT-I with cargo and other proteins of the ESCRT machinery to efficiently coordinate cargo sorting and release of ESCRT-I from the MVB.

Address correspondence to: Markus Babst (babst{at}biology.utah.edu)




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