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Interaction of Rho‐kinase with myosin II at stress fibres
Author(s) -
Kawabata Saeko,
Usukura Jiro,
Morone Nobuhiro,
Ito Masaaki,
Iwamatsu Akihiro,
Kaibuchi Kozo,
Amano Mutsuki
Publication year - 2004
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1356-9597.2004.00749.x
Subject(s) - pleckstrin homology domain , myosin light chain kinase , biology , myosin , biochemistry , irs1 , microbiology and biotechnology , phosphorylation , insulin receptor , insulin resistance , insulin , endocrinology
Rho‐kinase and myosin phosphatase cooperatively regulate the phosphorylation level of myosin light chain and are involved in the formation of stress fibres and smooth muscle contraction. Rho‐kinase has been known to be localized at stress fibres, but little is known about the mechanism of its localization. Here we identified non‐muscle myosin heavy chain IIA and IIB as the pleckstrin homology domain‐interacting molecules by affinity column chromatography. The pleckstrin homology domain of Rho‐kinase binds to myosin II directly in in vitro cosedimentation assay. The C‐terminal region of the pleckstrin homology domain was important for this interaction, and the point mutations in the pleckstrin homology domain mutant (W1170A, W1340L) resulted in a decrease in the binding. We also found that the pleckstrin homology domain, but not the pleckstrin homology domain mutant (W1170A, W1340L), was localized at stress fibres in fibroblasts. These results indicate that Rho‐kinase is localized at stress fibres through binding of the pleckstrin homology domain to myosin II.