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FEBS letters v.385 no.3, 1996년, pp.221 - 224  

Characterization of the interaction between RhoA and the amino-terminal region of PKN

Shibata, Hideki (Department of Biology, Faculty of Science, Kobe University, 1-1, Rokkodai-cho, Nada-ku, Kobe 657, Japan ); Mukai, Hideyuki ( Department of Biology, Faculty of Science, Kobe University, 1-1, Rokkodai-cho, Nada-ku, Kobe 657, Japan ); Inagaki, Yoshimasa ( Pharmaceutical Research Laboratory, Kirin Brewery Co. Ltd., 2-2, Souja-machi 1-choume, Maebashi 371, Japan ); Homma, Yoshimi ( Department of Biomolecular Sciences, Institute of Biomedical Sciences, Fukushima Medical College, 1 Hikarigaoka, Fukushima 960-12, Japan ); Kimura, Kazushi ( Division of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-01, Japan ); Kaibuchi, Kozo ( Division of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-01, Japan ); Narumiya, Shuh ( Department of Pharmacology, Kyoto University Faculty of Medicine, Yoshida, Sakyou-ku, Kyoto 606, Japan ); Ono, Yoshitaka ( Corresponding author. Fax: (81) (78) 803-0322. );
  • 초록  

    Abstract The yeast two-hybrid system and in vitro binding assay were carried out to characterize the interaction between PKN and a small GTP-binding protein, RhoA. It was revealed that the region corresponding to the amino acid residues 33–111 in the amino-terminal region of PKN was sufficient to confer the ability to associate with RhoA. Each synthetic peptide fragment corresponding to the amino acid residues 74–93 and 94–113 of PKN inhibited the interaction between PKN and RhoA in the in vitro binding assay, suggesting that this region is important in the association with RhoA. The endogenous and the GAP-stimulated GTPase activity of RhoA was inhibited by the interaction with PKN, suggesting the presence of a regulatory mechanism that sustains the GTP-bound active form of RhoA.


  • 주제어

    Serine/threonine protein kinase .   PKN .   Small GTP-binding protein .   RhoA .   GTP hydrolysis.  

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