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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/16009

Title: Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.
Authors: Mizutani, Takeomi Browse this author
Haga, Hisashi Browse this author →KAKEN DB
Koyama, Yoshikazu Browse this author
Takahashi, Masayuki Browse this author →KAKEN DB
Kawabata, Kazushige Browse this author
Issue Date: Dec-2006
Publisher: Wiley-Liss, Inc.
Journal Title: Journal of Cellular Physiology
Volume: 209
Issue: 3
Start Page: 726
End Page: 731
Publisher DOI: 10.1002/jcp.20773
PMID: 16924661
Abstract: 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.
Rights: Copyright © 2006 Wiley-Liss, Inc., Journal of Cellular Physiology,209(3), Pages 726 - 731
Relation: http://www.interscience.wiley.com/
Type: article (author version)
URI: http://hdl.handle.net/2115/16009
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 水谷 武臣

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