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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 |
2008-12-22
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pubmed:abstractText |
Arf (ADP-ribosylation factor) family small G proteins are crucial regulators of intracellular transport. The active GTP-bound form of Arf interacts with a set of proteins--effectors--which mediate the downstream signalling events of Arf activation. A well-studied class of Arf1 effectors comprises the coat complexes, such as the cis-Golgi-localized COPI (coat protein complex I) coat, and trans-Golgi network-endosomal clathrin coats. At least five different coats require Arf1-GTP to localize to organelle membranes. How a single Arf protein recruits different coat complexes to distinct membrane sites raises the question of how specificity is achieved. Here, we propose a molecular mechanism of this specificity for the COPI coat by showing a direct and specific interaction between a COPI subunit and a cis-Golgi localized subfamily of Arf guanine nucleotide exchange factors (GEFs) that takes place independently of Arf1 activation. In this way, a specific output on Arf1 activation can be programmed before the exchange reaction by the GEF itself.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-10198630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-10866202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-11809827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-12728274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-12967569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14527408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14654833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14690497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14690595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14729954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-14742722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-15616190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-15671486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-15717927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-15930122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-17041781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-17506703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-17640864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-17666033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-17850229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19039328-18003980
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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/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Coat Protein Complex I,
http://linkedlifedata.com/resource/pubmed/chemical/GEA1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/GEA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1469-3178
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
58-64
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:19039328-ADP-Ribosylation Factor 1,
pubmed-meshheading:19039328-ADP-Ribosylation Factors,
pubmed-meshheading:19039328-Animals,
pubmed-meshheading:19039328-Brefeldin A,
pubmed-meshheading:19039328-Cell Line,
pubmed-meshheading:19039328-Cercopithecus aethiops,
pubmed-meshheading:19039328-Coat Protein Complex I,
pubmed-meshheading:19039328-Enzyme Activation,
pubmed-meshheading:19039328-Golgi Apparatus,
pubmed-meshheading:19039328-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:19039328-Humans,
pubmed-meshheading:19039328-Protein Binding,
pubmed-meshheading:19039328-Protein Subunits,
pubmed-meshheading:19039328-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19039328-Time Factors
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pubmed:year |
2009
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pubmed:articleTitle |
A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor.
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pubmed:affiliation |
Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, NIH, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Intramural
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