Source:http://linkedlifedata.com/resource/pubmed/id/10229581
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1999-7-16
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pubmed:abstractText |
Eukaryotic vesicular transport requires the recognition of membranes through specific protein complexes. The heterotetrameric adaptor protein complexes 1, 2, and 3 (AP1/2/3) are composed of two large, one small, and one medium adaptin subunit. We isolated and characterized the cDNA for Arabidopsis gamma-adaptin and performed a phylogenetic analysis of all adaptin subunits (proteins) in the context of all known homologous proteins. This analysis revealed (i) that the large subunits of AP1/2/3 are homologous and (ii) two subunits of the heptameric coatomer I (COPI) complex belong to this gene family. In addition, all small subunits and the aminoterminal domain of the medium subunits of the heterotetramers are homologous to each other; this also holds for two corresponding subunits of the COPI complex. AP1/2/3 and a substructure (heterotetrameric, F-COPI subcomplex) of the heptameric COPI had a common ancestral complex (called pre-F-COPI). Since all large and all small/medium subunits share sequence similarity, the ancestor of this complex is inferred to have been a heterodimer composed of one large and one small subunit. The situation encountered today is the result of successive rounds of coordinated gene duplications of both the large and the small/medium subunits, with F-COPI being the first that separated from the ancestral pre-F-COPI.
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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 alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex gamma...,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Coatomer Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2844
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
770-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10229581-Adaptor Protein Complex 1,
pubmed-meshheading:10229581-Adaptor Protein Complex alpha Subunits,
pubmed-meshheading:10229581-Adaptor Protein Complex gamma Subunits,
pubmed-meshheading:10229581-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:10229581-Arabidopsis,
pubmed-meshheading:10229581-Biological Transport,
pubmed-meshheading:10229581-Coated Vesicles,
pubmed-meshheading:10229581-Coatomer Protein,
pubmed-meshheading:10229581-Eukaryotic Cells,
pubmed-meshheading:10229581-Evolution, Molecular,
pubmed-meshheading:10229581-Membrane Proteins,
pubmed-meshheading:10229581-Phylogeny
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pubmed:year |
1999
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pubmed:articleTitle |
Phylogenetic analysis of components of the eukaryotic vesicle transport system reveals a common origin of adaptor protein complexes 1, 2, and 3 and the F subcomplex of the coatomer COPI.
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pubmed:affiliation |
Botanical Institute, Technical University of Braunschweig, Humboldtstrasse 1, 38106 Braunschweig, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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