Identification of a putative target for Rho as the serine-threonine kinase protein kinase N

Mutsuki Amano, Hideyuki Mukai, Yoshitaka Ono, Kazuyasu Chihara, Takeshi Matsui, Yuko Hamajima, Katsuya Okawa, Akihiro Iwamatsu, Kozo Kaibuchi

研究成果: ジャーナルへの寄稿学術論文査読

397 被引用数 (Scopus)

抄録

Rho, a Ras-like small guanosine triphosphatase, has been implicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid (LPA) to form stress fibers and focal contacts. The form of RhoA bound to guanosine triphosphate directly bound to and activated a serine-threonine kinase, protein kinase N (PKN). Activated RhoA formed a complex with PKN and activated it in COS-7 cells. PKN was phosphorylated in Swiss 3T3 cells stimulated with LPA, and this phosphorylation was blocked by treatment of cells with botulinum C3 exoenzyme. Activation of Rho may be linked directly to a serine-threonine kinase pathway.

本文言語英語
ページ(範囲)648-650
ページ数3
ジャーナルScience
271
5249
DOI
出版ステータス出版済み - 02-02-1996
外部発表はい

All Science Journal Classification (ASJC) codes

  • 一般

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