| pubmed-article:12361576 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C1421563 | lld:lifeskim |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C2003913 | lld:lifeskim |
| pubmed-article:12361576 | lifeskim:mentions | umls-concept:C0056080 | lld:lifeskim |
| pubmed-article:12361576 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:12361576 | pubmed:dateCreated | 2002-10-3 | lld:pubmed |
| pubmed-article:12361576 | pubmed:abstractText | The functionality of the actin cytoskeleton depends on a dynamic equilibrium between filamentous and monomeric actin. Proteins of the ADF/cofilin family are essential for the high rates of actin filament turnover observed in motile cells through regulation of actin polymerization/depolymerization cycles. Rho GTPases act through p21-activated kinase-1 (Pak-1) and Rho kinase to inhibit cofilin activity via the LIM kinase (LIMK)-mediated phosphorylation of cofilin on Ser3. We report the identification of 14-3-3zeta as a novel phosphocofilin binding protein involved in the maintenance of the cellular phosphocofilin pool. A Ser3 phosphocofilin binding protein was purified from bovine brain and was identified as 14-3-3zeta by mass spectrometry. The phosphorylation-dependent interaction between cofilin and 14-3-3zeta was confirmed in pulldown and coimmunoprecipitation experiments. Both Ser3 phosphorylation and a 14-3-3 recognition motif in cofilin are necessary for 14-3-3 binding. The expression of 14-3-3zeta increases phosphocofilin levels, and the coexpression of 14-3-3zeta with LIMK further elevates phosphocofilin levels and potentiates LIMK-dependent effects on the actin cytoskeleton. This potentiation of cofilin action appears to be a result of the protection of phosphocofilin from phosphatase-mediated dephosphorylation at Ser3 by bound 14-3-3zeta. Taken together, these results suggest that 14-3-3zeta proteins may play a dynamic role in the regulation of cellular actin structures through the maintenance of phosphocofilin levels. | lld:pubmed |
| pubmed-article:12361576 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12361576 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12361576 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12361576 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12361576 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12361576 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12361576 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:12361576 | pubmed:author | pubmed-author:BokochGary... | lld:pubmed |
| pubmed-article:12361576 | pubmed:author | pubmed-author:GohlaAntjeA | lld:pubmed |
| pubmed-article:12361576 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12361576 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12361576 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:12361576 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12361576 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12361576 | pubmed:pagination | 1704-10 | lld:pubmed |
| pubmed-article:12361576 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12361576 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12361576 | pubmed:articleTitle | 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. | lld:pubmed |
| pubmed-article:12361576 | pubmed:affiliation | Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:12361576 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12361576 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12361576 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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