RRC ID 42739
Author Mizutani T, Haga H, Koyama Y, Takahashi M, Kawabata K.
Title Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.
Journal J Cell Physiol
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.
Volume 209(3)
Pages 726-31
Published 2006-12-1
DOI 10.1002/jcp.20773
PMID 16924661
MeSH Animals Cells, Cultured Fibroblasts / cytology* Fibroblasts / drug effects Fibroblasts / metabolism* Humans Intracellular Signaling Peptides and Proteins / genetics Intracellular Signaling Peptides and Proteins / metabolism Lysophospholipids / pharmacology Mice Myosin Light Chains / genetics Myosin Light Chains / metabolism* NIH 3T3 Cells Phosphorylation Protein Serine-Threonine Kinases / genetics Protein Serine-Threonine Kinases / metabolism Recombinant Fusion Proteins / genetics Recombinant Fusion Proteins / metabolism Stress Fibers / metabolism* Stress, Mechanical Tensile Strength rho-Associated Kinases rhoA GTP-Binding Protein / genetics rhoA GTP-Binding Protein / metabolism
IF 5.546
Times Cited 42
WOS Category PHYSIOLOGY CELL BIOLOGY
Resource
Human and Animal Cells NIH3T3