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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2005-4-1
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pubmed:abstractText |
The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10--a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.
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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/ACTR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ACTR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/ARHGAP10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ARHGAP21 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Actin-Related Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Actin-Related Protein 3,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
353-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15793564-ADP-Ribosylation Factor 1,
pubmed-meshheading:15793564-Actin-Related Protein 2,
pubmed-meshheading:15793564-Actin-Related Protein 3,
pubmed-meshheading:15793564-Actins,
pubmed-meshheading:15793564-Cytoskeletal Proteins,
pubmed-meshheading:15793564-GTPase-Activating Proteins,
pubmed-meshheading:15793564-Golgi Apparatus,
pubmed-meshheading:15793564-Guanosine Triphosphate,
pubmed-meshheading:15793564-HeLa Cells,
pubmed-meshheading:15793564-Humans,
pubmed-meshheading:15793564-Macromolecular Substances,
pubmed-meshheading:15793564-Signal Transduction,
pubmed-meshheading:15793564-Time Factors,
pubmed-meshheading:15793564-cdc42 GTP-Binding Protein
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pubmed:year |
2005
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pubmed:articleTitle |
Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics.
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pubmed:affiliation |
Membrane and Cytoskeleton Dynamics Group, Institut Curie, CNRS-UMR144, 75248 Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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