期刊
JOURNAL OF CELL BIOLOGY
卷 164, 期 3, 页码 427-439出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200306172
关键词
cell migration; cell polarity; membrane protrusion; MLCK; myosin phosphorylation
类别
资金
- NCI NIH HHS [R37 CA042742, R01 CA042742, CA42742] Funding Source: Medline
- NHLBI NIH HHS [R01 HL023615, HL23615] Funding Source: Medline
We examined the role of regulatory myosin light chain (MLC) phosphorylation of myosin II in cell migration of fibroblasts. Myosin light chain kinase (MLCK) inhibition blocked MLC phosphorylation at the cell periphery, but not in the center. MLCK-inhibited cells did not assemble zyxin-containing adhesions at the periphery, but maintained focal adhesions in the center. They generated membrane protrusions all around the cell, turned more frequently, and migrated less effectively. In contrast, Rho-associated kinase (ROCK) inhibition blocked MLC phosphorylation in the center, but not at the periphery. ROCK-inhibited cells assembled zyxin-containing adhesions at the periphery, but not focal adhesions in the center. They moved faster and more straight. On the other hand, inhibition of myosin phosphatase increased MLC phosphorylation and blocked peripheral membrane ruffling, as well as turnover of focal adhesions and cell migration. Our results suggest that myosin II activated by MLCK at the cell periphery controls membrane ruffling, and that the spatial regulation of MLC phosphorylation plays critical roles in controlling cell migration of fibroblasts.
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