Journal
JOURNAL OF CELL BIOLOGY
Volume 151, Issue 2, Pages 297-309Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.151.2.297
Keywords
Saccharomyces cerevisiae; vps; protein sorting; endosome; Golgi
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Funding
- NIGMS NIH HHS [GM53449] Funding Source: Medline
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Resident late-Golgi membrane proteins in Saccharomyces cerevisiae are selectively retrieved from a prevacuolar-endosomal compartment, a process dependent on aromatic amino acid-based sorting determinants on their cytosolic domains. The formation of retrograde vesicles from the prevacuolar compartment and the selective recruitment of vesicular cargo are thought to be mediated by a peripheral membrane retromer protein complex. We previously described mutations in one of the retromer subunit proteins, Vps35p, which caused cargo-specific defects in retrieval. By genetic and biochemical means we now show that Vps35p directly associates with the cytosolic domains of cargo proteins, Chemical cross-linking, followed by coimmunoprecipitation, demonstrated that Vps35p interacts with the cytosolic domain of A-ALP, a model late-Golgi membrane protein, in a retrieval signal-dependent manner. Furthermore, mutations in the cytosolic domains of A-ALP and another cargo protein, Vps10p, were identified that suppressed cargo-specific mutations in Vps35p bur did not suppress the retrieval defects of a vps35 null mutation. Suppression was shown to be due to an improvement in protein sorting at the prevacuolar compartment. These data strongly support a model in which Vps35p acts as a receptor protein for recognition of the retrieval signal domains of cargo proteins during their recruitment into retrograde vesicles.
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