Distinct regions of Galpha13 participate in its regulatory interactions with RGS homology domain-containing RhoGEFs.

@article{Kreutz2007DistinctRO,
  title={Distinct regions of Galpha13 participate in its regulatory interactions with RGS homology domain-containing RhoGEFs.},
  author={Barry Kreutz and Nicole Hajicek and Douglas M Yau and Susumu Nakamura and Tohru Kozasa},
  journal={Cellular signalling},
  year={2007},
  volume={19 8},
  pages={1681-9}
}
Galpha12 and Galpha13 transduce signals from G protein-coupled receptors to RhoA through RhoGEFs containing an RGS homology (RH) domain, such as p115 RhoGEF or leukemia-associated RhoGEF (LARG). The RH domain of p115 RhoGEF or LARG binds with high affinity to active forms of Galpha12 and Galpha13 and confers specific GTPase-activating protein (GAP) activity, with faster GAP responses detected in Galpha13 than in Galpha12. At the same time, Galpha13, but not Galpha12, directly stimulates the… CONTINUE READING

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