| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.59797585 |
| These results provide the first demonstration of a Ca ( 2+ ) dependent interaction between RGS 4 and CaM in vivo and show that association in lipid rafts of the plasma membrane might be involved in this physiological regulation of RGS proteins . . 0.59797585^^^ |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| Ca2+ / calmodulin does not directly affect GAP activity of RGS 4 but reverses PA and PIP 3 mediated inhibition . ^^^ |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| Indeed , Ca ( 2+ ) / calmodulin binds a complex of RGS 4 and a transition state analog of Galpha ( i 1 ) GDP AlF ( 4 ) ( ) . ^^^ |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| It is also abolished when a calmodulin inhibitor or a mutant RGS 4 is applied that can bind to calmodulin but that does not accelerate GTPase activity . ^^^ |
|
| Interacting proteins: P49798 and P62158 |
Pubmed |
SVM Score :0.0 |
| The GTPase accelerating activity of cardiac RGS proteins , such as RGS 4 , is inhibited by PtdIns ( 3 , 4 , 5 ) P 3 ( phosphatidylinositol 3 , 4 , 5 trisphosphate ) and this inhibition is cancelled by Ca2+ / calmodulin ( CaM ) formed during membrane depolarization . ^^^ Using lipid protein co sedimentation assay and surface plasmon resonance measurements , we show in the present study that the control of the GTPase accelerating activity of the RGS 4 protein is achieved through the competitive binding of PtdIns ( 3 , 4 , 5 ) P 3 and Ca2+ / CaM within its RGS domain . ^^^ |
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