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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-4-13
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pubmed:abstractText |
The GGAs constitute a family of modular adaptor-related proteins that bind ADP-ribosylation factors (ARFs) and localize to the trans-Golgi network (TGN) via their GAT domains. Here, we show that binding of the GAT domain stabilizes membrane-bound ARF1.GTP due to interference with the action of GTPase-activating proteins. We also show that the hinge and ear domains of the GGAs interact with clathrin in vitro, and that the GGAs promote recruitment of clathrin to liposomes in vitro and to TGN membranes in vivo. These observations suggest that the GGAs could function to link clathrin to membrane-bound ARF.GTP.
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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/ADP-Ribosylation Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/GGA adaptor proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-102
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11301005-ADP-Ribosylation Factor 1,
pubmed-meshheading:11301005-ADP-Ribosylation Factors,
pubmed-meshheading:11301005-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:11301005-Animals,
pubmed-meshheading:11301005-Carrier Proteins,
pubmed-meshheading:11301005-Cattle,
pubmed-meshheading:11301005-Clathrin,
pubmed-meshheading:11301005-Conserved Sequence,
pubmed-meshheading:11301005-GTP Phosphohydrolases,
pubmed-meshheading:11301005-GTPase-Activating Proteins,
pubmed-meshheading:11301005-Genes, Reporter,
pubmed-meshheading:11301005-Guanosine Triphosphate,
pubmed-meshheading:11301005-HeLa Cells,
pubmed-meshheading:11301005-Humans,
pubmed-meshheading:11301005-Intracellular Membranes,
pubmed-meshheading:11301005-Liposomes,
pubmed-meshheading:11301005-Protein Binding,
pubmed-meshheading:11301005-Protein Structure, Tertiary,
pubmed-meshheading:11301005-Protein Transport,
pubmed-meshheading:11301005-Sequence Homology, Amino Acid,
pubmed-meshheading:11301005-Structure-Activity Relationship,
pubmed-meshheading:11301005-Transfection,
pubmed-meshheading:11301005-trans-Golgi Network
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pubmed:year |
2001
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pubmed:articleTitle |
The GGAs promote ARF-dependent recruitment of clathrin to the TGN.
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pubmed:affiliation |
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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