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

doi:10.1016/0014-5793(96)00385-7

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

Research output: Contribution to journal › Article › peer-review

59 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 language	English
Pages (from-to)	221-224
Number of pages	4
Journal	FEBS Letters
Volume	385
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(96)00385-7
Publication status	Published - 06-05-1996
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(96)00385-7

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@article{163b7812083b4c0788711d655c83235c,

title = "Characterization of the interaction between RhoA and the amino-terminal region of PKN",

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.",

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

note = "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.",

year = "1996",

month = may,

day = "6",

doi = "10.1016/0014-5793(96)00385-7",

language = "English",

volume = "385",

pages = "221--224",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

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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

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SN - 0014-5793

VL - 385

SP - 221

EP - 224

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

Abstract

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