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The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole.
Cowles, C R; Odorizzi, G; Payne, G S; Emr, S D.
Affiliation
  • Cowles CR; Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California, San Diego 92093-0668, USA.
Cell ; 91(1): 109-18, 1997 Oct 03.
Article in En | MEDLINE | ID: mdl-9335339
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.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Vacuoles / Fungal Proteins / Saccharomyces cerevisiae Proteins / Monomeric Clathrin Assembly Proteins / Alkaline Phosphatase Type of study: Prognostic_studies Language: En Journal: Cell Year: 1997 Document type: Article Affiliation country: United States Country of publication: United States
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Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Vacuoles / Fungal Proteins / Saccharomyces cerevisiae Proteins / Monomeric Clathrin Assembly Proteins / Alkaline Phosphatase Type of study: Prognostic_studies Language: En Journal: Cell Year: 1997 Document type: Article Affiliation country: United States Country of publication: United States