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

Hideki Shibata, Hideyuki Mukai, Yoshimasa Inagaki, Yoshimi Homma, Kazushi Kimura, Kozo Kaibuchi, Shuh Narumiya, Yoshitaka Ono

研究成果: Article査読

58 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)221-224
ページ数4
ジャーナルFEBS Letters
385
3
DOI
出版ステータスPublished - 06-05-1996
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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