Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits.

@article{Mervine2006AnalysisOG,
  title={Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits.},
  author={Stacy M. Mervine and Evan A. Yost and Jonathan L. Sabo and Thomas R. Hynes and Catherine H. Berlot},
  journal={Molecular pharmacology},
  year={2006},
  volume={70 1},
  pages={194-205}
}
The specificity of G protein betagamma signaling demonstrated by in vivo knockouts is greater than expected based on in vitro assays of betagamma function. In this study, we investigated the basis for this discrepancy by comparing the abilities of seven beta1gamma complexes containing gamma1, gamma2, gamma5, gamma7, gamma10, gamma11, or gamma12 to interact with alphas and of these gamma subunits to compete for interaction with beta1 in live human embryonic kidney (HEK) 293 cells. betagamma… CONTINUE READING
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