G beta 5.RGS7 inhibits G alpha q-mediated signaling via a direct protein-protein interaction.

@article{Witherow2003GB5,
  title={G beta 5.RGS7 inhibits G alpha q-mediated signaling via a direct protein-protein interaction.},
  author={D. Scott Witherow and Steven C Tovey and Qiang Wang and Gary B. Willars and Vladlen Z Slepak},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 23},
  pages={21307-13}
}
A subfamily of regulators of G protein signaling (RGS) proteins consisting of RGS6, -7, -9, and -11 is characterized by the presence of a unique Ggamma-like domain through which they form obligatory dimers with the G protein subunit Gbeta5 in vivo. In Caenorhabditis elegans, orthologs of Gbeta5.RGS dimers are implicated in regulating both Galphai and Galphaq signaling, and in cell-based assays these dimers regulate Galphai/o- and Galphaq/11-mediated pathways. However, initial studies with… CONTINUE READING

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