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MBC in Press, published online ahead of print December 6, 2006
Mol. Biol. Cell 10.1091/mbc.E06-07-0601

A more recent version of this article appeared on February 1, 2007
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Submitted on July 17, 2006
Revised on October 23, 2006
Accepted on November 22, 2006

Mvb12 Is a Novel Member of ESCRT-I Involved in Cargo Selection by the MVB Pathway

Andrea J. Oestreich,* Brian A. Davies,* Johanna A. Payne, and David J. Katzmann

Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905

Monitoring Editor: Sandra Lemmon

The multivesicular body (MVB) sorting pathway impacts a variety of cellular functions in eukaryotic cells. Perhaps the best understood role for the MVB pathway is the degradation of transmembrane proteins within the lysosome. Regulation of cargo selection by this pathway is critically important for normal cell physiology, and recent advances in our understanding of this process have highlighted the endosomal sorting complexes required for transport (ESCRTs) as pivotal players in this reaction. To better understand the mechanisms of cargo selection during MVB sorting, we performed a genetic screen to identify novel factors required for cargo-specific selection by this pathway and identified the Mvb12 protein. Loss of Mvb12 function results in differential defects in the selection of MVB cargoes. A variety of analyses indicate that Mvb12 is a stable member of ESCRT-I, a heterologous complex involved in cargo selection by the MVB pathway. Phenotypes displayed upon loss of Mvb12 are distinct from those displayed by the previously described ESCRT-I subunits (Vps23, 28, and 37), suggesting a distinct function than these core subunits. These data support a model in which Mvb12 impacts the selection of MVB cargoes by modulating the cargo recognition capabilities of ESCRT-I.

*These authors contributed equally to this work.

Address correspondence to: David J. Katzmann (katzmann.david{at}mayo.edu)




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