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G protein beta gamma subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of gamma

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Iñiguez-Lluhi, J.A., Simon, M.I., Robishaw, J.D., Gilman, A.G.·1992·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)50106-x
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Abstract

Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) consist of a nucleotide-binding alpha subunit and a high-affinity complex of beta and gamma subunits. There is molecular heterogeneity of beta and gamma, but the significance of this diversity is poorly understood. Different G protein beta and gamma subunits have been expressed both singly and in combinations in Sf9 cells. Although expression of individual subunits is achieved in all cases, beta gamma subunit activity (support of pertussis toxin-catalyzed ADP-ribosylation of rGi alpha 1) is detected only when beta and gamma are expressed concurrently. Of the six combinations of beta gamma tested (beta 1 or beta 2 with gamma 1, gamma 2, or gamma 3), only one, beta 2 gamma 1, failed to generate a functional complex. Each of the other five complexes has been purified by subunit exchange chromatography using Go alpha-agarose as the chromatographic matrix. We have detected differences in the abilities of the purified proteins to support ADP-ribosylation of Gi alpha 1; these differences are attributable to the gamma component of the complex. When assayed for their ability to inhibit calmodulin-stimulated type-I adenylylcyclase activity or to potentiate Gs alpha-stimulated type-II adenylylcyclase, recombinant beta 1 gamma 1 and transducin beta gamma are approximately 10 and 20 times less potent, respectively, than the other complexes examined. Prenylation and/or further carboxyl-terminal processing of gamma are not required for assembly of the beta gamma subunit complex but are indispensable for high affinity interactions of beta gamma with either G protein alpha subunits or adenylylcyclases.

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Metadata

Authors
Iñiguez-Lluhi, J. A., Simon, M. I., Robishaw, J. D., & Gilman, A. G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-11
Volume
267
Issue
32
Pages
23409-23417
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)50106-x
OpenAlex
W1604834232
Cited by
305
References
1
FWCI
10.94
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: G protein beta gamma subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of gamma. https://app.cochat.ai/papers/10.1016/s0021-9258(18)50106-x
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Iñiguez-Lluhi, J. A., Simon, M. I., Robishaw, J. D., & Gilman, A. G. (1992). G protein beta gamma subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of gamma. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)50106-x

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