Protein Kinase N (PKN) and PKN-Related Protein Rhophilin as Targets of Small GTPase Rho
| Autor: | Akira Kakizuka, Narito Morii, Yoshitaka Ono, Hideyuki Mukai, Kazuko Fujisawa, Toshimasa Ishizaki, Pascal Madaule, Go Watanabe, Shuh Narumiya, Y. Saito |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
rho GTP-Binding Proteins
Recombinant Fusion Proteins Molecular Sequence Data Guanosine Saccharomyces cerevisiae GTPase Protein Serine-Threonine Kinases Guanosine triphosphate Biology Cell Line GTP Phosphohydrolases Mice chemistry.chemical_compound GTP-Binding Proteins RhoB GTP-Binding Protein Animals Humans Small GTPase Amino Acid Sequence Cloning Molecular Phosphorylation rhoB GTP-Binding Protein Protein kinase A Protein Kinase C Adaptor Proteins Signal Transducing Multidisciplinary Binding protein Membrane Proteins Enzyme Activation Biochemistry chemistry rhoC GTP-Binding Protein ras Proteins Guanosine Triphosphate rhoA GTP-Binding Protein RhoC GTP-Binding Protein Signal Transduction |
| Zdroj: | Science. 271:645-648 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|