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Cited by 417

The DOI matches its Crossref record.

Identification of a Putative Target for Rho as the Serine-Threonine Kinase Protein Kinase N

Amano, Mutsuki, Mukai, Hideyuki, Ono, Yoshitaka, Chihara, Kazuyasu, Matsui, Takeshi, Hamajima, Yuko, Okawa, Katsuya, Iwamatsu, Akihiro, Kaibuchi, Kozo·1996·Science
DOI 10.1126/science.271.5249.648
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Abstract

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.

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Metadata

Authors
Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., & Kaibuchi, K.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1996-02-02
Volume
271
Issue
5249
Pages
648-650
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.271.5249.648
OpenAlex
W2054246670
Cited by
417
References
0
FWCI
20.29
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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