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