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Genes to Cells (2004) 9, 653-660. doi:10.1111/j.1356-9597.2004.00749.x
© 2004 Blackwell Publishing or its licensors
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Interaction of Rho-kinase with myosin II at stress fibres

Saeko Kawabata1, Jiro Usukura2, Nobuhiro Morone2, Masaaki Ito3, Akihiro Iwamatsu4, Kozo Kaibuchi1 and Mutsuki Amano1,*

1 Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi 466-8550, Japan
2 Department of Anatomy and Cell Biology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi 466-8550, Japan
3 First Department of Internal Medicine, Mie University School of Medicine, Tsu, Mie 514-8507, Japan
4 Central Laboratories for Key Technology, Kirin Brewery Company Limited, Yokohama, Kanagawa 236-0004, Japan

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.

Communicated by: Noriko Osumi

* Correspondence: E-mail: m-amano{at}med.nagoya-u.ac.jp




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