Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP binding protein Rho

Takeshi Matsui, Mutsuki Amano, Takaharu Yamamoto, Kazuyasu Chihara, Masato Nakafuku, Masaaki Ito, Takeshi Nakano, Katsuya Okawa, Akihiro Iwamatsu, Kozo Kaibuchi

Research output: Contribution to journalArticlepeer-review

899 Citations (Scopus)

Abstract

The small GTP binding protein Rho is implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid to form stress fibers and focal contacts. Here we have purified a Rho-interacting protein with a molecular mass of ~ 164 kDa (p164) from bovine brain. This protein bound to GTPγS (a non-hydrolyzable GTP analog)·RhoA but not to GDP·RhoA or GTPγS·RhoA with a mutation in the effector domain (RhoA(A37)). p164 had a kinase activity which was specifically stimulated by GTPγS·RhoA. We obtained the cDNA encoding p164 on the basis of its partial amino acid sequences and named it Rho-associated kinase (Rho-kinase). Rho-kinase has a catalytic domain in the N-terminal portion, a coiled coil domain in the middle portion and a zinc finger-like motif in the C-terminal portion. The catalytic domain shares 72% sequence homology with that of myotonic dystrophy kinase and the coiled coil domain contains a Rho-interacting interface. When COS7 cells were co-transfected with Rho-kinase and activated RhoA, some Rho-kinase was recruited to membranes. Thus it is likely that Rho-kinase is a putative target serine/threonine kinase for Rho and serves as a mediator of the Rho-dependent signaling pathway.

Original languageEnglish
Pages (from-to)2208-2216
Number of pages9
JournalEMBO Journal
Volume15
Issue number9
DOIs
Publication statusPublished - 01-05-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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