Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-11-3
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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/CPS1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin A, http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl-Peptidases and..., 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/PEP12 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/STE13 protein, S cerevisiae, 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/clathrin assembly protein AP180
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-18
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9335339-Adaptor Protein Complex alpha Subunits, pubmed-meshheading:9335339-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:9335339-Alkaline Phosphatase, pubmed-meshheading:9335339-Biological Transport, pubmed-meshheading:9335339-Carboxypeptidases, pubmed-meshheading:9335339-Cathepsin A, pubmed-meshheading:9335339-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:9335339-Fungal Proteins, pubmed-meshheading:9335339-Golgi Apparatus, pubmed-meshheading:9335339-Lysosomes, pubmed-meshheading:9335339-Membrane Proteins, pubmed-meshheading:9335339-Monomeric Clathrin Assembly Proteins, pubmed-meshheading:9335339-Qa-SNARE Proteins, pubmed-meshheading:9335339-Recombinant Fusion Proteins, pubmed-meshheading:9335339-Saccharomyces cerevisiae, pubmed-meshheading:9335339-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9335339-Sequence Deletion, pubmed-meshheading:9335339-Vacuoles
pubmed:year
1997
pubmed:articleTitle
The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole.
pubmed:affiliation
Division of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California, San Diego 92093-0668, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't