FAK/src-family dependent activation of the Ste20-like kinase SLK is required for microtubule-dependent focal adhesion turnover and cell migration
Autor: | Simona Wagner, Kristin Roovers, Chris J. Storbeck, Luc A. Sabourin, Ziad Y. Chaar, Marlene McKay, Piotr Kolodziej |
---|---|
Rok vydání: | 2007 |
Předmět: |
Proto-Oncogene Proteins pp60(c-src)
lcsh:Medicine RAC1 Protein Serine-Threonine Kinases Microtubules Models Biological 3T3 cells Cell Biology/Cell Signaling Focal adhesion 03 medical and health sciences Mice 0302 clinical medicine Microtubule Cell Movement medicine Animals Phosphorylation RNA Small Interfering lcsh:Science Paxillin 030304 developmental biology 0303 health sciences Focal Adhesions Multidisciplinary biology lcsh:R Cell migration 3T3 Cells Fibroblasts Cell biology Cell Biology/Cell Adhesion medicine.anatomical_structure 030220 oncology & carcinogenesis Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases biology.protein lcsh:Q Signal transduction biological phenomena cell phenomena and immunity Proto-oncogene tyrosine-protein kinase Src Signal Transduction Research Article |
Zdroj: | PLoS ONE PLoS ONE, Vol 3, Iss 4, p e1868 (2008) |
ISSN: | 1932-6203 |
Popis: | Cell migration involves a multitude of signals that converge on cytoskeletal reorganization, essential for development, immune responses and tissue repair. Using knockdown and dominant negative approaches, we show that the microtubule-associated Ste20-like kinase SLK is required for focal adhesion turnover and cell migration downstream of the FAK/c-src complex. Our results show that SLK co-localizes with paxillin, Rac1 and the microtubules at the leading edge of migrating cells and is activated by scratch wounding. SLK activation is dependent on FAK/c-src/MAPK signaling, whereas SLK recruitment to the leading edge is src-dependent but FAK independent. Our results show that SLK represents a novel focal adhesion disassembly signal. |
Databáze: | OpenAIRE |
Externí odkaz: |