Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.
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概要
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Regulation of the contractile force is crucial for cell migration, cell proliferation, and maintenance of cell morphology. Phosphorylation of the myosin II regulatory light chain (MRLC) is involved in these processes. To show whether the diphosphorylation of MRLC increases the tension acting on stress fibers, changes in the stiffness of fibroblasts expressing wild-type MRLC and a mutant type, which cannot be diphosphorylated, on treatment with lysophosphatidic acid (LPA) were examined by a mechanical-scanning probe microscope (M-SPM). The LPA treatment increased cellular stiffness in the wild-type MRLC expressing cells, while it had no effect on the mutated cells. Immunostaining showed that LPA stimulation induced the diphosphorylation of MRLC. These results suggest that the diphosphorylation of MRLC enhances the tension acting on stress fibers. J. Cell. Physiol. 209: 726-731, 2006. © 2006 Wiley-Liss, Inc.
- Wiley-Liss, Inc.の論文
著者
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Kawabata K
Division Of Physics Graduate School Of Science Hokkaido University
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Haga H
Div. Of Biological Sciences Graduate School Of Sci. Hokkaido Univ.
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Haga Hisashi
北海道大学 生物化学科
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Haga Hisashi
Department Of Physics Faculty Of Science Hokkaido University
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Mizutani Takeomi
Transdisciplinary Life Science Course Faculty Of Advanced Life Science Hokkaido University
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