DOI: 10.1146/annurev.pharmtox.37.1.167. G PROTEIN βγ SUBUNITS

10.1146/annurev.pharmtox.37.1.167

Crossref journal-article

Annual Reviews

Annual Review of Pharmacology and Toxicology (22)

Abstract

▪ Abstract Guanine nucleotide binding (G) proteins relay extracellular signals encoded in light, small molecules, peptides, and proteins to activate or inhibit intracellular enzymes and ion channels. The larger G proteins, made up of Gαβγ heterotrimers, dissociate into Gα and Gβγ subunits that separately activate intracellular effector molecules. Only recently has the Gβγ subunit been recognized as a signal transduction molecule in its own right; Gβγ is now known to directly regulate as many different protein targets as the Gα subunit. Recent X-ray crystallography of Gα, Gβγ, and Gαβγ subunits will guide the investigation of structure-function relationships.

Bibliography

Clapham, D. E., & Neer, E. J. (1997). G PROTEIN Î²Î³ SUBUNITS. Annual Review of Pharmacology and Toxicology, 37(1), 167â203.

Authors 2

David E. Clapham (first)
Eva J. Neer (additional)

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Dates

Type	When
Created	23 years ago (July 27, 2002, 7:45 a.m.)
Deposited	3 years, 10 months ago (Oct. 16, 2021, 3:04 a.m.)
Indexed	3 weeks, 5 days ago (July 30, 2025, 8:22 p.m.)
Issued	28 years, 4 months ago (April 1, 1997)
Published	28 years, 4 months ago (April 1, 1997)
Published Print	28 years, 4 months ago (April 1, 1997)

Funders 0

None

BibTeX

@article{Clapham_1997, title={G PROTEIN βγ SUBUNITS}, volume={37}, ISSN={1545-4304}, url={http://dx.doi.org/10.1146/annurev.pharmtox.37.1.167}, DOI={10.1146/annurev.pharmtox.37.1.167}, number={1}, journal={Annual Review of Pharmacology and Toxicology}, publisher={Annual Reviews}, author={Clapham, David E. and Neer, Eva J.}, year={1997}, month=apr, pages={167–203} }

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  "abstract": "<jats:p> \u25aa Abstract\u2002 Guanine nucleotide binding (G) proteins relay extracellular signals encoded in light, small molecules, peptides, and proteins to activate or inhibit intracellular enzymes and ion channels. The larger G proteins, made up of G<jats:sub>\u03b1\u03b2\u03b3</jats:sub> heterotrimers, dissociate into G<jats:sub>\u03b1</jats:sub> and G<jats:sub>\u03b2\u03b3</jats:sub> subunits that separately activate intracellular effector molecules. Only recently has the G<jats:sub>\u03b2\u03b3</jats:sub> subunit been recognized as a signal transduction molecule in its own right; G<jats:sub>\u03b2\u03b3</jats:sub> is now known to directly regulate as many different protein targets as the G<jats:sub>\u03b1</jats:sub> subunit. Recent X-ray crystallography of G<jats:sub>\u03b1</jats:sub>, G<jats:sub>\u03b2\u03b3</jats:sub>, and G<jats:sub>\u03b1\u03b2\u03b3</jats:sub> subunits will guide the investigation of structure-function relationships. </jats:p>",
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