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