An alliance between Ras GTPase-activating protein, filamin C, and Ras GTPase-activating protein SH3 domain-binding protein regulates myocyte growth
| Autor: | Ieng-Yi Chen, Jacqueline Lypowy, Maha Abdellatif |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
GTPase-activating protein
Cell Survival Filamins Apoptosis Biology Filamin Biochemistry SH3 domain Rats Sprague-Dawley src Homology Domains Mice Contractile Proteins Cyclin-dependent kinase Two-Hybrid System Techniques Protein biosynthesis Animals Myocytes Cardiac Poly-ADP-Ribose Binding Proteins Molecular Biology Kinase Binding protein Ribosomal Protein S6 Kinases Microfilament Proteins DNA Helicases Cell Biology Molecular biology Actins Cyclin-Dependent Kinases Rats RNA Recognition Motif Proteins ras GTPase-Activating Proteins biology.protein Cyclin-dependent kinase 7 Carrier Proteins Cell Division RNA Helicases |
| Zdroj: | The Journal of biological chemistry. 280(27) |
| ISSN: | 0021-9258 |
| Popis: | We have previously reported that Ras GTPase-activating protein (RasGAP) is involved in a pathway that regulates total cellular mRNA and protein synthesis in cardiac myocytes. A yeast two-hybrid screen resulted in identification of filamin C (FLN-C) as one of its targets. Knockdown of RasGAP or FLN-C, or severing their interaction, resulted in down-regulation of the RNA polymerase II kinase, cyclin-dependent kinase 7 (Cdk7). This appeared to be provoked by the release of cdk7 mRNA from RasGAP SH3 domain-binding protein, G3BP, and its subsequent degradation. In parallel, myocyte growth was also inhibited. On the other hand, overexpression of RasGAP induced a Cdk7- and FLN-C-dependent growth. Thus, we propose that the physical interaction between RasGAP and FLN-C facilitates an interaction between G3BP and cdk7 mRNA. This results in stabilization of cdk7 mRNA, an increase in its protein, which is required for cell growth. |
| Databáze: | OpenAIRE |
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