Gβ5 prevents the RGS7-Gαo interaction through binding to a distinct Gγ-like domain found in RGS7 and other RGS proteins
10.1073/pnas.96.5.2503
Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

The G protein β subunit Gβ5 deviates significantly from the other four members of Gβ-subunit family in amino acid sequence and subcellular localization. To detect the protein targets of Gβ5 in vivo , we have isolated a native Gβ5 protein complex from the retinal cytosolic fraction and identified the protein tightly associated with Gβ5 as the regulator of G protein signaling (RGS) protein, RGS7. Here we show that complexes of Gβ5 with RGS proteins can be formed in vitro from the recombinant proteins. The reconstituted Gβ5-RGS dimers are similar to the native retinal complex in their behavior on gel-filtration and cation-exchange chromatographies and can be immunoprecipitated with either anti-Gβ5 or anti-RGS7 antibodies. The specific Gβ5-RGS7 interaction is determined by a distinct domain in RGS that has a striking homology to Gγ subunits. Deletion of this domain prevents the RGS7-Gβ5 binding, although the interaction with Gα is retained. Substitution of the Gγ-like domain of RGS7 with a portion of Gγ1 changes its binding specificity from Gβ5 to Gβ1. The interaction of Gβ5 with RGS7 blocked the binding of RGS7 to the Gα subunit Gαo, indicating that Gβ5 is a specific RGS inhibitor.

Bibliography

Levay, K., Cabrera, J. L., Satpaev, D. K., & Slepak, V. Z. (1999). Gβ5 prevents the RGS7-Gαo interaction through binding to a distinct Gγ-like domain found in RGS7 and other RGS proteins. Proceedings of the National Academy of Sciences, 96(5), 2503–2507.

Authors 4
  1. Konstantin Levay (first)
  2. Jorge L. Cabrera (additional)
  3. Daulet K. Satpaev (additional)
  4. Vladlen Z. Slepak (additional)
References 30 Referenced 83
  1. V Y Arshavsky, M D Bownds Nature (London) 357, 416–417 (1992). (10.1038/357416a0) / Nature (London) by Arshavsky V Y (1992)
  2. G Berstein, J L Blank, D Y Jhon, J H Exton, S G Rhee, E M Ross Cell 70, 411–418 (1992). (10.1016/0092-8674(92)90165-9) / Cell by Berstein G (1992)
  3. H G Dohlman, J Thorner J Biol Chem 272, 3871–3874 (1997). (10.1074/jbc.272.7.3871) / J Biol Chem by Dohlman H G (1997)
  4. V Y Arshavsky, E N Pugh Neuron 20, 11–14 (1998). (10.1016/S0896-6273(00)80430-4) / Neuron by Arshavsky V Y (1998)
  5. D M Berman, A G Gilman J Biol Chem 273, 1269–1272 (1998). (10.1074/jbc.273.3.1269) / J Biol Chem by Berman D M (1998)
  6. S Popov, K Yu, T Kozasa, T M Wilkie Proc Natl Acad Sci USA 94, 7216–7220 (1997). (10.1073/pnas.94.14.7216) / Proc Natl Acad Sci USA by Popov S (1997)
  7. E Faurobert, J B Hurley Proc Natl Acad Sci USA 94, 2945–2950 (1997). (10.1073/pnas.94.7.2945) / Proc Natl Acad Sci USA by Faurobert E (1997)
  8. B E Snow, R A Hall, A M Krumins, G M Brothers, D Bouchard, C A Brothers, S Chung, J Mangion, A G Gilman, R J Lefkowitz, D P Siderovski J Biol Chem 273, 17749–17755 (1998). (10.1074/jbc.273.28.17749) / J Biol Chem by Snow B E (1998)
  9. T Kozasa, X Jiang, M J Hart, P M Sternweis, W D Singer, A G Gilman, G Bollag, P C Sternweis Science 280, 2109–2111 (1998). (10.1126/science.280.5372.2109) / Science by Kozasa T (1998)
  10. J L Cabrera, F de Freitas, D K Satpaev, V Z Slepak Biochim Biophys Res Commun 249, 898–902 (1998). (10.1006/bbrc.1998.9218) / Biochim Biophys Res Commun by Cabrera J L (1998)
  11. J A Watson, A Katz, M I Simon J Biol Chem 269, 22150–22156 (1994). (10.1016/S0021-9258(17)31768-4) / J Biol Chem by Watson J A (1994)
  12. J A Watson, A M Aragay, V Z Slepak, M I Simon J Biol Chem 271, 28154–28160 (1996). (10.1074/jbc.271.45.28154) / J Biol Chem by Watson J A (1996)
  13. S Zhang, O A Coso, C Lee, J S Gutkind, W F Simonds J Biol Chem 271, 33575–33579 (1996). (10.1074/jbc.271.52.33575) / J Biol Chem by Zhang S (1996)
  14. M L Bayewitch, T Avidor-Reiss, R Levy, T Pfeuffer, I Nevo, W F Simonds, Z Vogel J Biol Chem 273, 2273–2276 (1998). (10.1074/jbc.273.4.2273) / J Biol Chem by Bayewitch M L (1998)
  15. J E Fletcher, M A Lindorfer, J M DeFilippo, H Yasuda, M Guilmard, J C Garrison J Biol Chem 273, 636–644 (1998). (10.1074/jbc.273.1.636) / J Biol Chem by Fletcher J E (1998)
  16. W He, C W Cowan, T G Wensel Neuron 20, 95–102 (1998). (10.1016/S0896-6273(00)80437-7) / Neuron by He W (1998)
  17. M R Koelle, H R Horvitz Cell 84, 115–125 (1996). (10.1016/S0092-8674(00)80998-8) / Cell by Koelle M R (1996)
  18. B E Snow, A M Krumins, G M Brothers, S F Lee, M A Wall, S Chung, J Mangion, S Arya, A G Gilman, D P Siderovski Proc Natl Acad Sci USA 95, 13307–13312 (1998). (10.1073/pnas.95.22.13307) / Proc Natl Acad Sci USA by Snow B E (1998)
  19. C J Schmidt, E J Neer J Biol Chem 266, 4538–4544 (1991). (10.1016/S0021-9258(20)64356-3) / J Biol Chem by Schmidt C J (1991)
  20. C J Schmidt, T C Thomas, M A Levine, E J Neer J Biol Chem 267, 13807–13810 (1992). (10.1016/S0021-9258(19)49638-5) / J Biol Chem by Schmidt C J (1992)
  21. D M Berman, T Kozasa, A G Gilman J Biol Chem 271, 27209–27212 (1996). (10.1074/jbc.271.44.27209) / J Biol Chem by Berman D M (1996)
  22. D E Clapham, E J Neer Nature (London) 365, 403–406 (1993). (10.1038/365403a0) / Nature (London) by Clapham D E (1993)
  23. E Neer, T F Smith Cell 84, 175–178 (1996). (10.1016/S0092-8674(00)80969-1) / Cell by Neer E (1996)
  24. C E Ford, N P Skiba, H Bae, Y Daaka, E Reuveny, L R Shekter, R Rosal, G Weng, C S Yang, R Iyengar, et al. Science 280, 1271–1274 (1998). (10.1126/science.280.5367.1271) / Science by Ford C E (1998)
  25. E J Neer, C J Schmidt, R Nambudripad, T F Smith Nature (London) 371, 297–300 (1994). (10.1038/371297a0) / Nature (London) by Neer E J (1994)
  26. S J Gold, Y G Ni, H G Dohlman, E J Nestler J Neurosci 17, 8024–8037 (1997). (10.1523/JNEUROSCI.17-20-08024.1997) / J Neurosci by Gold S J (1997)
  27. D J Pepperl, S Shah-Basu, D VanLeeuwen, J G Granneman, R G MacKenzie Biochem Biophys Res Commun 243, 52–55 (1998). (10.1006/bbrc.1997.8056) / Biochem Biophys Res Commun by Pepperl D J (1998)
  28. E A Thomas, P E Danielson, J G Sutcliffe J Neurosci Res 52, 118–124 (1998). (10.1002/(SICI)1097-4547(19980401)52:1<118::AID-JNR11>3.0.CO;2-6) / J Neurosci Res by Thomas E A (1998)
  29. C P Ponting, P Bork Trends Biochem Sci 21, 245–246 (1996). (10.1016/S0968-0004(96)30027-3) / Trends Biochem Sci by Ponting C P (1996)
  30. B Yu, V Z Slepak, M I Simon J Biol Chem 272, 18015–18021 (1997). (10.1074/jbc.272.29.18015) / J Biol Chem by Yu B (1997)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 10:32 a.m.)
Deposited 3 years, 2 months ago (June 7, 2022, 12:27 a.m.)
Indexed 3 months, 1 week ago (May 20, 2025, 9:50 a.m.)
Issued 26 years, 5 months ago (March 2, 1999)
Published 26 years, 5 months ago (March 2, 1999)
Published Online 26 years, 5 months ago (March 2, 1999)
Published Print 26 years, 5 months ago (March 2, 1999)
Funders 0

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@article{Levay_1999, title={Gβ5 prevents the RGS7-Gαo interaction through binding to a distinct Gγ-like domain found in RGS7 and other RGS proteins}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.5.2503}, DOI={10.1073/pnas.96.5.2503}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Levay, Konstantin and Cabrera, Jorge L. and Satpaev, Daulet K. and Slepak, Vladlen Z.}, year={1999}, month=mar, pages={2503–2507} }