Literature DB >> 9335339

The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole.

C R Cowles1, G Odorizzi, G S Payne, S D Emr.   

Abstract

Three distinct adaptor protein (AP) complexes involved in protein trafficking have been identified. AP-1 and AP-2 mediate protein sorting at the trans-Golgi network and plasma membrane, respectively, whereas the function of AP-3 has not been defined. A screen for factors specifically involved in transport of alkaline phosphatase (ALP) from the Golgi to the vacuole/lysosome has identified Ap16p and Ap15p of the yeast AP-3 complex. Deletion of each of the four AP-3 subunits results in selective mislocalization of ALP and the vacuolar t-SNARE, Vam3p (but not CPS and CPY), while deletion of AP-1 and AP-2 subunits has no effect on vacuolar protein delivery. This study, therefore, provides evidence that the AP-3 complex functions in cargo-selective protein transport from the Golgi to the vacuole/lysosome.

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Year:  1997        PMID: 9335339     DOI: 10.1016/s0092-8674(01)80013-1

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  172 in total

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5.  Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes.

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Journal:  Mol Biol Cell       Date:  2002-03       Impact factor: 4.138

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8.  The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface.

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Journal:  Proc Natl Acad Sci U S A       Date:  2002-05-07       Impact factor: 11.205

9.  Effects on vesicular transport pathways at the late endosome in cells with limited very long-chain fatty acids.

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10.  Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking.

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