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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
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pubmed:dateCreated |
1997-7-14
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pubmed:databankReference | |
pubmed:abstractText |
Recent studies have described a widely expressed adaptor-like complex, named AP-3, which is likely involved in protein sorting in exocytic/endocytic pathways. The AP-3 complex is composed of four distinct subunits. Here, we report the identification of one of the subunits of this complex, which we call beta3A-adaptin. The predicted amino acid sequence of beta3A-adaptin reveals that the protein is closely related to the neuron-specific protein beta-NAP (61% overall identity) and more distantly related to the beta1- and beta2-adaptin subunits of the clathrin-associated adaptor complexes AP-1 and AP-2, respectively. Sequence comparisons also suggest that beta3A-adaptin has a domain organization similar to beta-NAP and to beta1- and beta2-adaptins. beta3A-adaptin is expressed in all tissues and cells examined. Co-purification and co-precipitation analyses demonstrate that beta3A-adaptin corresponds to the approximately 140-kDa subunit of the ubiquitous AP-3 complex, the other subunits being delta-adaptin, p47A (now called mu3A) and sigma3 (A or B). beta3A-adaptin is phosphorylated on serine residues in vivo while the other subunits of the complex are not detectably phosphorylated. beta3A-adaptin is not present in significant amounts in clathrin-coated vesicles. The characteristics of beta3A-adaptin reported here lend support to the idea that AP-3 is a structural and functional homolog of the clathrin-associated adaptors AP-1 and AP-2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex 1,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex 3,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex beta...,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15078-84
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9182526-Adaptor Protein Complex 1,
pubmed-meshheading:9182526-Adaptor Protein Complex 3,
pubmed-meshheading:9182526-Adaptor Protein Complex beta Subunits,
pubmed-meshheading:9182526-Amino Acid Sequence,
pubmed-meshheading:9182526-Clathrin,
pubmed-meshheading:9182526-Cloning, Molecular,
pubmed-meshheading:9182526-DNA, Complementary,
pubmed-meshheading:9182526-DNA-Binding Proteins,
pubmed-meshheading:9182526-Membrane Proteins,
pubmed-meshheading:9182526-Molecular Sequence Data,
pubmed-meshheading:9182526-RNA, Messenger,
pubmed-meshheading:9182526-Sequence Homology, Amino Acid,
pubmed-meshheading:9182526-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
Beta3A-adaptin, a subunit of the adaptor-like complex AP-3.
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pubmed:affiliation |
Cell Biology and Metabolism Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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