pubmed-article:9822597 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C0072074 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C1155950 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:9822597 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:9822597 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:9822597 | pubmed:dateCreated | 1999-1-13 | lld:pubmed |
pubmed-article:9822597 | pubmed:abstractText | Profilin was first identified as an actin monomer binding protein; however, recent reports indicate its involvement in actin polymerization. To date, there is no direct evidence of a functional role in vivo for profilin in actin cytoskeletal reorganization. Here, we prepared a profilin mutant (H119E) defective in actin binding, but retaining the ability to bind to other proteins. This mutant profilin I suppresses actin polymerization in microspike formation induced by N-WASP, the essential factor in microspike formation. Profilin associates both in vivo and in vitro with N-WASP at proline-rich sites different from those to which Ash/Grb2 binds. This association between profilin and N-WASP is required for N-WASP-induced efficient microspike elongation. Moreover, we succeeded in reconstituting microspike formation in permeabilized cells using profilin I combined with N-WASP and its regulator, Cdc42. These findings provide the first evidence that profilin is a key molecule linking a signaling network to rapid actin polymerization in microspike formation. | lld:pubmed |
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pubmed-article:9822597 | pubmed:language | eng | lld:pubmed |
pubmed-article:9822597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9822597 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9822597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9822597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9822597 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9822597 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9822597 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:9822597 | pubmed:author | pubmed-author:TakenawaTT | lld:pubmed |
pubmed-article:9822597 | pubmed:author | pubmed-author:MikiHH | lld:pubmed |
pubmed-article:9822597 | pubmed:author | pubmed-author:SuetsuguSS | lld:pubmed |
pubmed-article:9822597 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9822597 | pubmed:day | 16 | lld:pubmed |
pubmed-article:9822597 | pubmed:volume | 17 | lld:pubmed |
pubmed-article:9822597 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9822597 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9822597 | pubmed:pagination | 6516-26 | lld:pubmed |
pubmed-article:9822597 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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