Source:http://linkedlifedata.com/resource/pubmed/id/15688017
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2005-3-17
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| pubmed:abstractText |
Missing in metastasis (MIM) gene encodes an actin binding protein that is expressed at low levels in a subset of malignant cell lines. MIM protein tagged by green fluorescent protein (GFP) colocalizes with cortactin, an Arp2/3 complex activator, and interacts directly with the SH3 domain of cortactin. Recombinant full-length MIM promotes markedly cortactin and Arp2/3 complex-mediated actin polymerization in an SH3 dependent manner. In contrast, MIM-CT, a short splicing variant of MIM, binds poorly to cortactin in vitro and is unable to enhance actin polymerization. Full-length MIM binds to G-actin with a similar affinity as N-WASP-VCA, a constitutively active form of N-WASP, and inhibits N-WASP-VCA-mediated actin polymerization as analysed in vitro. The significance of the association of MIM with cortactin and G-actin was evaluated in NIH3T3 cells expressing several MIM constructs. Overexpression of full-length wild-type MIM-GFP inhibited markedly the motility of NIH3T3 cells induced by PDGF and that of human vein umbilical endothelial cells induced by sphingosine 1 phosphate. However, an MIM mutant with deletion of the WH2 domain, which is responsible for G-actin binding, enhanced cell motility. The motility inhibition imposed by MIM was compromised in the cells overexpressing N-WASP. In contrast, deletion of an MIM proline-rich domain, which is required for an optimal binding to cortactin, substantiated the MIM-mediated inhibition of cell motility. These data imply that MIM regulates cell motility by modulating different Arp2/3 activators in a distinguished manner.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cortactin,
http://linkedlifedata.com/resource/pubmed/chemical/Cttn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mtss1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Wasl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0950-9232
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
17
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| pubmed:volume |
24
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2059-66
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15688017-3T3 Cells,
pubmed-meshheading:15688017-Actins,
pubmed-meshheading:15688017-Animals,
pubmed-meshheading:15688017-Cell Line,
pubmed-meshheading:15688017-Cell Line, Tumor,
pubmed-meshheading:15688017-Cell Movement,
pubmed-meshheading:15688017-Cortactin,
pubmed-meshheading:15688017-Gene Expression Regulation,
pubmed-meshheading:15688017-Mice,
pubmed-meshheading:15688017-Microfilament Proteins,
pubmed-meshheading:15688017-Neoplasm Proteins,
pubmed-meshheading:15688017-Nerve Tissue Proteins,
pubmed-meshheading:15688017-Platelet-Derived Growth Factor,
pubmed-meshheading:15688017-Sequence Deletion,
pubmed-meshheading:15688017-Umbilical Veins,
pubmed-meshheading:15688017-Wiskott-Aldrich Syndrome Protein, Neuronal
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| pubmed:year |
2005
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| pubmed:articleTitle |
Differential regulation of cortactin and N-WASP-mediated actin polymerization by missing in metastasis (MIM) protein.
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| pubmed:affiliation |
Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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