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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-6-14
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1535-6108
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
575-85
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pubmed:dateRevised |
2009-12-11
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pubmed:meshHeading |
pubmed-meshheading:15193260-Alanine,
pubmed-meshheading:15193260-Apoptosis,
pubmed-meshheading:15193260-Blotting, Western,
pubmed-meshheading:15193260-Breast Neoplasms,
pubmed-meshheading:15193260-Carrier Proteins,
pubmed-meshheading:15193260-Cell Cycle,
pubmed-meshheading:15193260-Cell Division,
pubmed-meshheading:15193260-Cell Line, Tumor,
pubmed-meshheading:15193260-Cell Survival,
pubmed-meshheading:15193260-Cell Transformation, Neoplastic,
pubmed-meshheading:15193260-Drosophila Proteins,
pubmed-meshheading:15193260-Dyneins,
pubmed-meshheading:15193260-Flow Cytometry,
pubmed-meshheading:15193260-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:15193260-Glutathione Transferase,
pubmed-meshheading:15193260-Humans,
pubmed-meshheading:15193260-Immunohistochemistry,
pubmed-meshheading:15193260-Microscopy, Fluorescence,
pubmed-meshheading:15193260-Mutation,
pubmed-meshheading:15193260-Neoplasms,
pubmed-meshheading:15193260-Phenotype,
pubmed-meshheading:15193260-Phosphorylation,
pubmed-meshheading:15193260-Plasmids,
pubmed-meshheading:15193260-Protein Binding,
pubmed-meshheading:15193260-Protein Structure, Tertiary,
pubmed-meshheading:15193260-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15193260-Serine,
pubmed-meshheading:15193260-Signal Transduction,
pubmed-meshheading:15193260-Time Factors,
pubmed-meshheading:15193260-Two-Hybrid System Techniques,
pubmed-meshheading:15193260-Up-Regulation,
pubmed-meshheading:15193260-p21-Activated Kinases
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pubmed:year |
2004
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pubmed:articleTitle |
Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes.
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pubmed:affiliation |
Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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