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Protein Kinase N (PKN) and PKN-Related Protein Rhophilin as Targets of Small GTPase Rho
Abstract
The Rho guanosine 5′-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.
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Citations
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Metadata
- Authors
- Watanabe, G., Saito, Y., Madaule, P., Ishizaki, T., Fujisawa, K., Morii, N., Mukai, H., Ono, Y., Kakizuka, A., & Narumiya, S.
- Venue
- Science
- Published
- 1996-02-02
- Volume
- 271
- Issue
- 5249
- Pages
- 645-648
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2009394026
- Cited by
- 390
- References
- 0
- FWCI
- 22.14
- Type
- journal article
- Language
- en
- Open access
- closed
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