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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1999-7-29
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pubmed:abstractText |
The rapid modulation of ligand-binding affinity ("activation") is a central property of the integrin family of cell adhesion receptors. The small GTP-binding protein Ras and its downstream effector kinase Raf-1 suppress integrin activation. In this study we explored the relationship between Ras and the closely related small GTP-binding protein R-Ras in modulating the integrin affinity state. We found that R-Ras does not seem to be a direct activator of integrins in Chinese hamster ovary cells. However, we observed that GTP-bound R-Ras strongly antagonizes the Ras/Raf-initiated integrin suppression pathway. Furthermore, this reversal of the Ras/Raf suppressor pathway does not seem to be via a competition between Ras and R-Ras for common downstream effectors or via an inhibition of Ras/Raf-induced MAP kinase activation. Thus, R-Ras and Ras may act in concert to regulate integrin affinity via the activation of distinct downstream effectors.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-1555235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-1948065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-2100193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-2115210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-2411729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-2491843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-2642744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-3098437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-7510712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-7761090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-7809086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-7936652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8002932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8108110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8253074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8334704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8530488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8620538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8626420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8631302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8636068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8991288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-8999998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9010215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9032266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9038343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9050889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9150145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9311917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9362489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9566869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9728397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10359597-9852038
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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/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIIb-IIIa...,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/ral GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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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 |
1799-809
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10359597-Animals,
pubmed-meshheading:10359597-CHO Cells,
pubmed-meshheading:10359597-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10359597-Cricetinae,
pubmed-meshheading:10359597-GTP Phosphohydrolases,
pubmed-meshheading:10359597-GTP-Binding Proteins,
pubmed-meshheading:10359597-Guanosine Triphosphate,
pubmed-meshheading:10359597-Integrins,
pubmed-meshheading:10359597-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:10359597-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:10359597-Platelet Glycoprotein GPIIb-IIIa Complex,
pubmed-meshheading:10359597-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:10359597-Suppression, Genetic,
pubmed-meshheading:10359597-ral GTP-Binding Proteins,
pubmed-meshheading:10359597-ras Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway.
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pubmed:affiliation |
Department of Respiratory Medicine, University of Edinburgh Medical School, Edinburgh EH8 9AG, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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