Interaction of Rho-kinase with myosin II at stress fibres

Saeko Kawabata, Jiro Usukura, Nobuhiro Morone, Masaaki Ito, Akihiro Iwamatsu, Kozo Kaibuchi, Mutsuki Amano

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

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. Rhokinase 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.

Original languageEnglish
Pages (from-to)653-660
Number of pages8
JournalGenes to Cells
Volume9
Issue number7
DOIs
Publication statusPublished - 07-2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Cell Biology

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