| pubmed-article:12732638 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C2700384 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C0215407 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C0676792 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C0039082 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1412171 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1412400 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1421482 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1658596 | lld:lifeskim |
| pubmed-article:12732638 | lifeskim:mentions | umls-concept:C1705294 | lld:lifeskim |
| pubmed-article:12732638 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:12732638 | pubmed:dateCreated | 2003-7-4 | lld:pubmed |
| pubmed-article:12732638 | pubmed:abstractText | The WASP and cortactin families constitute two distinct classes of Arp2/3 modulators in mammalian cells. Physical and functional interactions among the Arp2/3 complex, VCA (a functional domain of N-WASP), and cortactin were examined under conditions that were with or without actin polymerization. In the absence of actin, cortactin binds significantly weaker to the Arp2/3 complex than VCA. At concentrations of VCA 20-fold lower than cortactin, the association of cortactin with the Arp2/3 complex was nearly abolished. Analysis of the cells infected with Shigella demonstrated that N-WASP located at the tip of the bacterium, whereas cortactin accumulated in the comet tail. Interestingly, cortactin promotes Arp2/3 complex-mediated actin polymerization and actin branching in the presence of VCA at a saturating concentration, and cortactin acquired 20 nm affinity for the Arp2/3 complex during actin polymerization. The interaction of VCA with the Arp2/3 complex was reduced in the presence of both cortactin and actin. Moreover, VCA reduced its affinity for Arp2/3 complex at branching sites that were stabilized by phalloidin. These data imply a novel mechanism for the de novo assembly of a branched actin network that involves a coordinated sequential interaction of N-WASP and cortactin with the Arp2/3 complex. | lld:pubmed |
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| pubmed-article:12732638 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12732638 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12732638 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12732638 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12732638 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12732638 | pubmed:author | pubmed-author:ZhanXiX | lld:pubmed |
| pubmed-article:12732638 | pubmed:author | pubmed-author:UrunoTakehito... | lld:pubmed |
| pubmed-article:12732638 | pubmed:author | pubmed-author:SmithNicoleN | lld:pubmed |
| pubmed-article:12732638 | pubmed:author | pubmed-author:LiuJialiJ | lld:pubmed |
| pubmed-article:12732638 | pubmed:author | pubmed-author:LiYansongY | lld:pubmed |
| pubmed-article:12732638 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12732638 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:12732638 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12732638 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12732638 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12732638 | pubmed:pagination | 26086-93 | lld:pubmed |
| pubmed-article:12732638 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12732638 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12732638 | pubmed:articleTitle | Sequential interaction of actin-related proteins 2 and 3 (Arp2/3) complex with neural Wiscott-Aldrich syndrome protein (N-WASP) and cortactin during branched actin filament network formation. | lld:pubmed |
| pubmed-article:12732638 | pubmed:affiliation | Department of Experimental Pathology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, Maryland 20855, USA. | lld:pubmed |
| pubmed-article:12732638 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12732638 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12732638 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12732638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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