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| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C1955933 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C0023693 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:15193260 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:15193260 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15193260 | pubmed:dateCreated | 2004-6-14 | lld:pubmed |
| pubmed-article:15193260 | pubmed:abstractText | We identified dynein light chain 1 (DLC1) as a physiologic substrate of p21-activated kinase 1 (Pak1). Pak1-DLC1 interaction plays an essential role in cell survival, which depends on Pak1's phosphorylation of DLC1 on Ser88. Pak1 associates with the complex of DLC1 and BimL, a proapoptotic BH3-only protein, and phosphorylates both proteins. Phosphorylation of BimL by Pak1 prevents it from interacting with and inactivation of Bcl-2, an antiapoptotic protein. Overexpression of DLC1 but not DLC1-Ser88Ala mutant promotes cancerous properties of breast cancer cells. DLC1 protein level is elevated in more than 90% of human breast tumors. The regulation of cell survival functions by Pak1-DLC1 interaction represents a novel mechanism by which a signaling kinase might regulate the cancerous phenotypes. | lld:pubmed |
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| pubmed-article:15193260 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15193260 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15193260 | pubmed:issn | 1535-6108 | lld:pubmed |
| pubmed-article:15193260 | pubmed:author | pubmed-author:KumarRakeshR | lld:pubmed |
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| pubmed-article:15193260 | pubmed:author | pubmed-author:YangZhiboZ | lld:pubmed |
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| pubmed-article:15193260 | pubmed:author | pubmed-author:BalasenthilSe... | lld:pubmed |
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| pubmed-article:15193260 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15193260 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:15193260 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15193260 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15193260 | pubmed:pagination | 575-85 | lld:pubmed |
| pubmed-article:15193260 | pubmed:dateRevised | 2009-12-11 | lld:pubmed |
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| pubmed-article:15193260 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15193260 | pubmed:articleTitle | Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. | lld:pubmed |
| pubmed-article:15193260 | pubmed:affiliation | Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA. | lld:pubmed |
| pubmed-article:15193260 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15193260 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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