FAK–Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
| Autor: | Leanna Whitmore, Alan F. Horwitz, Donna J. Webb, Karen Donais, Sheila M. Thomas, J. Thomas Parsons, Christopher E. Turner |
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| Rok vydání: | 2004 |
| Předmět: |
Myosin light-chain kinase
Role of cell adhesions in neural development Recombinant Fusion Proteins PTK2 Biology Focal adhesion Mice Cell Movement Cell Adhesion Animals Myosin-Light-Chain Kinase Paxillin Retinoblastoma-Like Protein p130 Proteins Cell migration Cell Biology Adhesion Fibroblasts Protein-Tyrosine Kinases Phosphoproteins Cell biology Adaptor Proteins Vesicular Transport Cytoskeletal Proteins Crk-Associated Substrate Protein src-Family Kinases Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases biology.protein Mitogen-Activated Protein Kinases Signal Transduction Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Nature Cell Biology. 6:154-161 |
| ISSN: | 1476-4679 1465-7392 |
| DOI: | 10.1038/ncb1094 |
| Popis: | Cell migration is a complex, highly regulated process that involves the continuous formation and disassembly of adhesions (adhesion turnover). Adhesion formation takes place at the leading edge of protrusions, whereas disassembly occurs both at the cell rear and at the base of protrusions. Despite the importance of these processes in migration, the mechanisms that regulate adhesion formation and disassembly remain largely unknown. Here we develop quantitative assays to measure the rate of incorporation of molecules into adhesions and the departure of these proteins from adhesions. Using these assays, we show that kinases and adaptor molecules, including focal adhesion kinase (FAK), Src, p130CAS, paxillin, extracellular signal-regulated kinase (ERK) and myosin light-chain kinase (MLCK) are critical for adhesion turnover at the cell front, a process central to migration. |
| Databáze: | OpenAIRE |
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