Source:http://linkedlifedata.com/resource/pubmed/id/15860728
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 9
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| pubmed:dateCreated |
2005-4-29
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| pubmed:abstractText |
Recent studies show that the partitioning of the small GTPase H-Ras in different types of membrane microdomains is dependent on guanosine 5'-triphosphate (GTP)-loading of H-Ras. Detailed knowledge about the in vivo dynamics of this phenomenon is limited. In this report, the effect of the activation of H-Ras on its microdomain localization was studied by single-molecule fluorescence microscopy. Individual human H-Ras molecules fused to the enhanced yellow fluorescent protein (eYFP) were imaged in the dorsal plasma membrane of live mouse cells and their diffusion behavior was analyzed. The diffusion of a constitutively inactive (S17N) and constitutively active (G12V) mutant of H-Ras was compared. Detailed analysis revealed that for both mutants a major, fast-diffusing population and a minor, slow-diffusing population were present. The slow-diffusing fraction of the active mutant was confined to 200 nm domains, which were not observed for the inactive mutant. In line with these results we observed that the slow-diffusing fraction of wild-type H-Ras became confined to 200 nm domains upon insulin-induced activation of wild-type H-Ras. This activation-dependent localization of H-Ras to 200 nm domains, for the first time directly detected in live cells, supports the proposed relationship between H-Ras microdomain localization and activation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
118
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1799-809
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:15860728-Animals,
pubmed-meshheading:15860728-Bacterial Proteins,
pubmed-meshheading:15860728-Biophysics,
pubmed-meshheading:15860728-Cell Line,
pubmed-meshheading:15860728-Cell Membrane,
pubmed-meshheading:15860728-Cytoskeleton,
pubmed-meshheading:15860728-Diffusion,
pubmed-meshheading:15860728-Fibroblasts,
pubmed-meshheading:15860728-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:15860728-Genes, ras,
pubmed-meshheading:15860728-Guanosine Triphosphate,
pubmed-meshheading:15860728-Humans,
pubmed-meshheading:15860728-Insulin,
pubmed-meshheading:15860728-Luminescent Proteins,
pubmed-meshheading:15860728-MAP Kinase Signaling System,
pubmed-meshheading:15860728-Mice,
pubmed-meshheading:15860728-Microscopy, Fluorescence,
pubmed-meshheading:15860728-Models, Statistical,
pubmed-meshheading:15860728-Mutation,
pubmed-meshheading:15860728-Plasmids,
pubmed-meshheading:15860728-Protein Structure, Tertiary,
pubmed-meshheading:15860728-Time Factors,
pubmed-meshheading:15860728-Transfection,
pubmed-meshheading:15860728-ras Proteins
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| pubmed:year |
2005
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| pubmed:articleTitle |
Single-molecule diffusion measurements of H-Ras at the plasma membrane of live cells reveal microdomain localization upon activation.
|
| pubmed:affiliation |
Department of Biophysics, Leiden Institute of Physics, Leiden University, Niels Bohrweg 2, 2333 CA Leiden, The Netherlands.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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