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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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RGS4  -  regulator of G-protein signaling 4

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High impact information on RGS4

  • RGS1, RGS4 and GAIP (for G alpha-interacting protein) bind specifically and tightly to G alphai and G alpha0 in cell membranes treated with GDP and AlF4(-), and are GAPs for G alphai, G alpha0 and transducin alpha-subunits, but not for G alphas [1].
  • A single mutation of Gs alpha, Asp229Ser, rendered the Gs alpha subunit with the ability to interact with RGS16 and RGS4 [2].
  • Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4 [3].
  • The GTPase-accelerating activity of cardiac RGS proteins, such as RGS4, is inhibited by PtdIns(3,4,5)P3 (phosphatidylinositol 3,4,5-trisphosphate) and this inhibition is cancelled by Ca2+/calmodulin (CaM) formed during membrane depolarization [4].
  • 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 RGS4 protein is achieved through the competitive binding of PtdIns(3,4,5)P3 and Ca2+/CaM within its RGS domain [4].

References

  1. RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Watson, N., Linder, M.E., Druey, K.M., Kehrl, J.H., Blumer, K.J. Nature (1996) [Pubmed]
  2. A single mutation Asp229 --> Ser confers upon Gs alpha the ability to interact with regulators of G protein signaling. Natochin, M., Artemyev, N.O. Biochemistry (1998) [Pubmed]
  3. Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Tesmer, V.M., Kawano, T., Shankaranarayanan, A., Kozasa, T., Tesmer, J.J. Science (2005) [Pubmed]
  4. Phosphatidylinositol 3,4,5-trisphosphate and Ca2+/calmodulin competitively bind to the regulators of G-protein-signalling (RGS) domain of RGS4 and reciprocally regulate its action. Ishii, M., Fujita, S., Yamada, M., Hosaka, Y., Kurachi, Y. Biochem. J. (2005) [Pubmed]
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