期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 456, 期 2, 页码 224-231出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2006.09.025
关键词
cell migration; myosin; myosin light chain kinase; rho; small GTPases; focal adhesions; mechanotransduction
资金
- NIGMS NIH HHS [GM-32476, R01 GM061806, R01 GM-61806, R37 GM032476, R01 GM032476] Funding Source: Medline
Adhesive cells show complex mechanical interactions with the substrate, however the exact mechanism of such interactions, termed traction forces, is still unclear. To address this question we have measured traction forces of fibroblasts treated with agents that affect the myosin II-dependent contractile mechanism. Using the potent myosin II inhibitor blebbistatin, we demonstrate that traction forces are strongly dependent on a functional myosin II heavy chain. Since myosin II is regulated by both the myosin light chain kinase (NILCK) and, directly or indirectly, the Rho-associated kinase (ROCK), we examined the effects of inhibitors against these kinases. Interestingly, inhibition of the myosin light chain kinase had no detectable effect, while inhibition of the Rho-dependent kinase caused strong inhibition of traction forces. Our results indicate that ROCK and NILCK play non-redundant roles in regulating myosin II functions, and that a subset of myosin II, regulated by the Rho small GTPase, may be responsible for the regulation of traction forces in migrating fibroblasts. (c) 2006 Elsevier Inc. All rights reserved.
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