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

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58 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)221-224
Number of pages4
JournalFEBS Letters
Volume385
Issue number3
DOIs
Publication statusPublished - 06-05-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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