QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 18, Issue 2, 636-645, February 2007

This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: E06-07-0588v1 18/2/636    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Curtiss, M. Articles by Babst, M. Search for Related Content PubMed PubMed Citation Articles by Curtiss, M. Articles by Babst, M.

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

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

Submitted July 10, 2006; Revised October 26, 2006; Accepted November 20, 2006
Monitoring Editor: Sandra Lemmon

The endosomal sorting complex required for transport (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 vacuolar protein sorting (Vps) 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 they did result 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.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-07-0588) on November 29, 2006.

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

Abbreviations used: ESCRT, endosomal sorting complex required for transport; MVB, multivesicular body; Vps, vacuolar protein sorting.

This article has been cited by other articles:

				S. B. Shields, A. J. Oestreich, S. Winistorfer, D. Nguyen, J. A. Payne, D. J. Katzmann, and R. Piper ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting J. Cell Biol., April 20, 2009; 185(2): 213 - 224. [Abstract] [Full Text] [PDF]

				C. Schluter, K. K.Y. Lam, J. Brumm, B. W. Wu, M. Saunders, T. H. Stevens, J. Bryan, and E. Conibear Global Analysis of Yeast Endosomal Transport Identifies the Vps55/68 Sorting Complex Mol. Biol. Cell, April 1, 2008; 19(4): 1282 - 1294. [Abstract] [Full Text] [PDF]

				C. Dimaano, C. B. Jones, A. Hanono, M. Curtiss, and M. Babst Ist1 Regulates Vps4 Localization and Assembly Mol. Biol. Cell, February 1, 2008; 19(2): 465 - 474. [Abstract] [Full Text] [PDF]

				B. McDonald and J. Martin-Serrano Regulation of Tsg101 Expression by the Steadiness Box: A Role of Tsg101-associated Ligase Mol. Biol. Cell, February 1, 2008; 19(2): 754 - 763. [Abstract] [Full Text] [PDF]