G proteins

John R. Hepler; Alfred G. Gilman

doi:10.1016/0968-0004(92)90005-T

G proteins

John R. Hepler, Alfred G. Gilman

Pharmacology

Research output: Contribution to journal › Article › peer-review

930 Scopus citations

Abstract

The family of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) serves an essential role in transducing receptor-generated signals across the plasma membrane. Recent findings reveal unexpected functional roles for individual G protein subunits. Thus, GTP-binding α-subunits and the βγ-subunit complex can influence the activity of effector molecules independently or simultaneously, either synergistically or in opposition, to elicit a complex constellation of cellular events.

Original language	English (US)
Pages (from-to)	383-387
Number of pages	5
Journal	Trends in biochemical sciences
Volume	17
Issue number	10
DOIs	https://doi.org/10.1016/0968-0004(92)90005-T
State	Published - Oct 1992

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Access to Document

10.1016/0968-0004(92)90005-T

Cite this

@article{d054d6a398584f9eb7777a2a836e120b,

title = "G proteins",

abstract = "The family of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) serves an essential role in transducing receptor-generated signals across the plasma membrane. Recent findings reveal unexpected functional roles for individual G protein subunits. Thus, GTP-binding α-subunits and the βγ-subunit complex can influence the activity of effector molecules independently or simultaneously, either synergistically or in opposition, to elicit a complex constellation of cellular events.",

author = "Hepler, {John R.} and Gilman, {Alfred G.}",

note = "Funding Information: The authors would like to thank M. Linder, T. Kozasa, J. l~iguez-Lluhi and N. Ueda for hlepful comments. Work from the authors' laboratory was supported by NIH Grant GM34497, American Cancer Society Grant BE30N, The Perot Family Foundation, The Lucille P. Markey Charitable Trust and The Raymond and Ellen Willie Chair of Molecular Neuropharmacology. J. R. H. is the recipient of a National Research Service Award F32 GM13569.",

year = "1992",

month = oct,

doi = "10.1016/0968-0004(92)90005-T",

language = "English (US)",

volume = "17",

pages = "383--387",

journal = "Trends in biochemical sciences",

issn = "0968-0004",

publisher = "Elsevier Limited",

number = "10",

}

TY - JOUR

T1 - G proteins

AU - Hepler, John R.

AU - Gilman, Alfred G.

N1 - Funding Information: The authors would like to thank M. Linder, T. Kozasa, J. l~iguez-Lluhi and N. Ueda for hlepful comments. Work from the authors' laboratory was supported by NIH Grant GM34497, American Cancer Society Grant BE30N, The Perot Family Foundation, The Lucille P. Markey Charitable Trust and The Raymond and Ellen Willie Chair of Molecular Neuropharmacology. J. R. H. is the recipient of a National Research Service Award F32 GM13569.

PY - 1992/10

Y1 - 1992/10

N2 - The family of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) serves an essential role in transducing receptor-generated signals across the plasma membrane. Recent findings reveal unexpected functional roles for individual G protein subunits. Thus, GTP-binding α-subunits and the βγ-subunit complex can influence the activity of effector molecules independently or simultaneously, either synergistically or in opposition, to elicit a complex constellation of cellular events.

AB - The family of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) serves an essential role in transducing receptor-generated signals across the plasma membrane. Recent findings reveal unexpected functional roles for individual G protein subunits. Thus, GTP-binding α-subunits and the βγ-subunit complex can influence the activity of effector molecules independently or simultaneously, either synergistically or in opposition, to elicit a complex constellation of cellular events.

UR - http://www.scopus.com/inward/record.url?scp=0026712877&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026712877&partnerID=8YFLogxK

U2 - 10.1016/0968-0004(92)90005-T

DO - 10.1016/0968-0004(92)90005-T

M3 - Article

C2 - 1455506

AN - SCOPUS:0026712877

SN - 0968-0004

VL - 17

SP - 383

EP - 387

JO - Trends in biochemical sciences

JF - Trends in biochemical sciences

IS - 10

ER -

G proteins

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this