期刊
CELL ADHESION & MIGRATION
卷 6, 期 4, 页码 302-306出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/cam.20488
关键词
nascent adhesion; focal adhesion kinase; talin; adhesion assembly; recruitment; focal adhesion turnover; motility; beta 1 integrin
类别
资金
- CIHR [200810MFE-193594-139144] Funding Source: Medline
- NCI NIH HHS [R01 CA102310, CA102310] Funding Source: Medline
- NHLBI NIH HHS [R01 HL093156, HL093156] Funding Source: Medline
- NIGMS NIH HHS [R01 GM087400, GM087400] Funding Source: Medline
Cell migration requires the coordination of adhesion site assembly and turnover. Canonical models for nascent adhesion formation postulate that integrin binding to extracellular matrix (ECM) proteins results in the rapid recruitment of cytoskeletal proteins such as talin and paxillin to integrin cytoplasmic domains. It is thought that integrin-talin clusters recruit and activate tyrosine kinases such as focal adhesion kinase (FAK). However, the molecular connections of this linkage remain unresolved. Our recent findings support an alternative model whereby FAK recruits talin to new sites of beta 1 integrin-mediated adhesion in mouse embryonic fibroblasts and human ovarian carcinoma cells. This is dependent on a direct binding interaction between FAK and talin and occurs independently of direct talin binding to beta 1 integrin. Herein, we discuss differences between nascent and mature adhesions, interactions between FAK, talin and paxillin, possible mechanisms of FAK activation and how this FAK-talin complex may function to promote cell motility through increased adhesion turnover.
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