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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-9-8
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pubmed:abstractText |
Transport of a subset of membrane proteins to the yeast vacuole requires the function of the AP-3 adaptor protein complex. To define the molecular requirements of vesicular transport in this pathway, we used a biochemical approach to analyse the formation and content of the AP-3 transport intermediate. A vam3tsf (vacuolar t-SNARE) mutant blocks vesicle docking and fusion with the vacuole and causes the accumulation of 50-130-nanometre membrane vesicles, which we isolated and showed by biochemical analysis and immunocytochemistry to contain both AP-3 adaptors and alkaline phosphatase (ALP) pathway cargoes. Inactivation of AP-3 or the protein Vps41 blocks formation of this vesicular intermediate. Vps41 binds to the AP-3 delta-adaptin subunit, suggesting that they function together in the formation of ALP pathway transport intermediates at the late Golgi.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric Clathrin Assembly Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NPL3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VAM3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/VPS41 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/clathrin assembly protein AP180
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
346-53
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pubmed:dateRevised |
2009-6-10
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pubmed:meshHeading |
pubmed-meshheading:10559961-Adaptor Protein Complex alpha Subunits,
pubmed-meshheading:10559961-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:10559961-Alkaline Phosphatase,
pubmed-meshheading:10559961-Binding Sites,
pubmed-meshheading:10559961-Biological Transport,
pubmed-meshheading:10559961-Carrier Proteins,
pubmed-meshheading:10559961-Cell Compartmentation,
pubmed-meshheading:10559961-Cell Membrane,
pubmed-meshheading:10559961-Fungal Proteins,
pubmed-meshheading:10559961-Membrane Proteins,
pubmed-meshheading:10559961-Monomeric Clathrin Assembly Proteins,
pubmed-meshheading:10559961-Mutagenesis,
pubmed-meshheading:10559961-Nuclear Proteins,
pubmed-meshheading:10559961-Qa-SNARE Proteins,
pubmed-meshheading:10559961-RNA-Binding Proteins,
pubmed-meshheading:10559961-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10559961-Vacuoles,
pubmed-meshheading:10559961-Vesicular Transport Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Formation of AP-3 transport intermediates requires Vps41 function.
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pubmed:affiliation |
Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California, San Diego, La Jolla, California 92093-0668, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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