| First Author | Watanabe G | Year | 1996 |
| Journal | Science | Volume | 271 |
| Issue | 5249 | Pages | 645-8 |
| PubMed ID | 8571126 | Mgi Jnum | J:40343 |
| Mgi Id | MGI:87684 | Doi | 10.1126/science.271.5249.645 |
| Citation | Watanabe G, et al. (1996) Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science 271(5249):645-8 |
| abstractText | 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. |
