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Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.
Mizutani, Takeomi; Haga, Hisashi; Koyama, Yoshikazu; Takahashi, Masayuki; Kawabata, Kazushige.
Afiliación
  • Mizutani T; Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita-ku, Sapporo 060-0810, Japan. mizutani@sci.hokudai.ac.jp
J Cell Physiol ; 209(3): 726-31, 2006 Dec.
Article en En | MEDLINE | ID: mdl-16924661
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cadenas Ligeras de Miosina / Fibras de Estrés / Fibroblastos Límite: Animals / Humans Idioma: En Revista: J Cell Physiol Año: 2006 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cadenas Ligeras de Miosina / Fibras de Estrés / Fibroblastos Límite: Animals / Humans Idioma: En Revista: J Cell Physiol Año: 2006 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos