TY - JOUR
T1 - Characterization of the interaction between RhoA and the amino-terminal region of PKN
AU - Shibata, Hideki
AU - Mukai, Hideyuki
AU - Inagaki, Yoshimasa
AU - Homma, Yoshimi
AU - Kimura, Kazushi
AU - Kaibuchi, Kozo
AU - Narumiya, Shuh
AU - Ono, Yoshitaka
N1 - Funding Information:
Acknowledgements." We thank Y. Nishizuka for encouragement. This work was supported in part by research grants from the Ministry of Education, Science, Sports, and Culture, Japan, the Senri Life Science Foundation, the Japan Foundation for Applied Enzymology, the San-kyo Foundation of Life Science, and Kirin Brewery Co., Ltd.
PY - 1996/5/6
Y1 - 1996/5/6
N2 - 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.
AB - 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.
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U2 - 10.1016/0014-5793(96)00385-7
DO - 10.1016/0014-5793(96)00385-7
M3 - Article
C2 - 8647255
AN - SCOPUS:0029938410
VL - 385
SP - 221
EP - 224
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -