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RGS4 and GAIP are GTPase-activating proteins for G qα and block activation of phospholipase Cβ by γ-thio-GTP-G qα
Open accessAbstract
RGS proteins constitute a newly appreciated and large group of negative r egulators of G protein s ignaling. Four members of the RGS family act as GTPase-activating proteins (GAPs) with apparent specificity for members of the G iα subfamily of G protein subunits. We demonstrate here that two RGS proteins, RGS4 and GAIP, also act as GAPs for G qα , the G α protein responsible for activation of phospholipase Cβ. Furthermore, these RGS proteins block activation of phospholipase Cβ by guanosine 5′-(3- O -thio)triphosphate-G qα . GAP activity does not explain this effect, which apparently results from occlusion of the binding site on G α for effector. Inhibitory effects of RGS proteins on G protein-mediated signaling pathways can be demonstrated by simple mixture of RGS4 or GAIP with plasma membranes.
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Cited by
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Winden, K. D., Oldham, M. C., Mirnics, K., Ebert, P. J., Swan, C. H., Levitt, P., Rubenstein, J. L., Horvath, S., & Geschwind, D. H. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.46 · Cited by 112
Liu, W., Yuen, E. Y., Allen, P. B., Feng, J., Greengard, P., & Yan, Z. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604560103 · Cited by 79
Paspalas, C. D., Selemon, L. D., & Arnsten, A. F. T. (2009) · Cerebral Cortex · doi:10.1093/cercor/bhn235 · Cited by 31
Metadata
- Authors
- Hepler, J. R., Berman, D. M., Gilman, A. G., & Kozasa, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-01-21
- Volume
- 94
- Issue
- 2
- Pages
- 428-432
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1614895539
- Cited by
- 360
- References
- 0
- FWCI
- 11.59
- Type
- journal article
- Language
- en
- Open access
- green
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- Hepler, J. R., Berman, D. M., Gilman, A. G., & Kozasa, T. (1997). RGS4 and GAIP are GTPase-activating proteins for G qα and block activation of phospholipase Cβ by γ-thio-GTP-G qα. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.2.428
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