| pubmed-article:20308062 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0258432 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C2004491 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0029219 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0017056 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1538325 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C0005495 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1547959 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:20308062 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:20308062 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:20308062 | pubmed:dateCreated | 2010-5-24 | lld:pubmed |
| pubmed-article:20308062 | pubmed:abstractText | The Arp2/3 complex is essential for actin filament nucleation in a variety of cellular processes. The activation of the Arp2/3 complex is mediated by nucleation-promoting factors, such as the Wiskott-Aldrich syndrome family proteins, which share a WCA (WH2 domain, central region, acidic region) catalytic module at the C-terminal region, required for Arp2/3 activation, but diverge at the N-terminal region, required for binding to specific activators. Here, we report the characterization of WASH, a new member of the WAS family that has nucleation-promoting factor activity and recently has been demonstrated to play a role in endosomal sorting. We found that overexpression of the WASH-WCA domain induced disruption of the actin cytoskeleton, whereas overexpression of full-length WASH in mammalian cells did not affect stress fiber organization. Furthermore, our analysis has revealed that nerve growth factor treatment of PC12 cells overexpressing full-length WASH leads to disruption of the actin cytoskeleton. We have also found that WASH interacts through its N-terminal region with BLOS2, a centrosomal protein belonging to the BLOC-1 complex that functions as a scaffolding factor in the biogenesis of lysosome-related organelles. In addition to BLOS2, WASH also interacts with centrosomal gamma-tubulin and with pallidin, an additional component of the BLOC-1 complex. Collectively, our data propose that WASH is a bimodular protein in which the C terminus is involved in Arp2/3-mediated actin nucleation, whereas the N-terminal portion is required for its regulation and localization in the cells. Moreover, our data suggest that WASH is also a component of the BLOC-1 complex that is associated with the centrosomes. | lld:pubmed |
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| pubmed-article:20308062 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20308062 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20308062 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20308062 | pubmed:month | May | lld:pubmed |
| pubmed-article:20308062 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20308062 | pubmed:author | pubmed-author:D'UrsoMichele... | lld:pubmed |
| pubmed-article:20308062 | pubmed:author | pubmed-author:LappalainenPe... | lld:pubmed |
| pubmed-article:20308062 | pubmed:author | pubmed-author:MonfregolaJle... | lld:pubmed |
| pubmed-article:20308062 | pubmed:author | pubmed-author:UrsiniMatilde... | lld:pubmed |
| pubmed-article:20308062 | pubmed:author | pubmed-author:NapolitanoGen... | lld:pubmed |
| pubmed-article:20308062 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20308062 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:20308062 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20308062 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20308062 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20308062 | pubmed:pagination | 16951-7 | lld:pubmed |
| pubmed-article:20308062 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
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| pubmed-article:20308062 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20308062 | pubmed:articleTitle | Functional characterization of Wiskott-Aldrich syndrome protein and scar homolog (WASH), a bi-modular nucleation-promoting factor able to interact with biogenesis of lysosome-related organelle subunit 2 (BLOS2) and gamma-tubulin. | lld:pubmed |
| pubmed-article:20308062 | pubmed:affiliation | Institute of Genetics and Biophysics Adriano Buzzati Traverso, 80131 Naples, Italy. | lld:pubmed |
| pubmed-article:20308062 | pubmed:publicationType | Journal Article | lld:pubmed |
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