Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts

• Takeomi Mizutani

• Hisashi Haga

• Yoshikazu Koyama

• Masayuki Takahashi

• Kazushige Kawabata

抄録

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.

収録刊行物

• Journal of Cellular Physiology

  Journal of Cellular Physiology 209 (3), 726-731, 2006-08-21

  Wiley

キーワード

• Cell Biology
• Clinical Biochemistry
• Physiology

詳細情報

• CRID: 1362544418857449344
• NII論文ID: 80018778048
• DOI: 10.1002/jcp.20773
• ISSN: 10974652
• ISSN: 00219541
• Web Site: https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjcp.20773
• Web Site: https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcp.20773
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