Regulatory GTP-binding proteins: Emerging concepts on their role in cell function

Irene Litosch

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

The last few years have evidenced a tremendous expansion in our appreciation of the role of regulatory GTP-binding proteins in cellular activation. The availability of cholera and pertussis toxins to detect G proteins as well as methodological advances in the study of cellular function has afforded the opportunity to examine G protein participation in many cellular events. Regulation of adenylyl cyclase and cyclic GMP phosphodiesterase by G proteins has been demonstrated. Phosphatidylinositol-4,5-bisphosphate specific phospholipase C activity appears to be subject to G protein control. G proteins regulate inward K+ and Ca2+ channels through a mechanism which may be independent of effects on the above mentioned enzymes. Certainly, the number of G proteins which have been identified from sequencing of complementary DNA affords the potential for G protein involvement in many cellular events. Only three G proteins have however been isolated and functionally characterized, Gs, Gi and transducin. Whether all the functions of these proteins have been identified remains to be seen.

Original languageEnglish
Pages (from-to)251-258
Number of pages8
JournalLife Sciences
Volume41
Issue number3
DOIs
StatePublished - Jul 20 1987
Externally publishedYes

Fingerprint

GTP-Binding Proteins
Transducin
Cholera Toxin
Cyclic GMP
Pertussis Toxin
Phosphoric Diester Hydrolases
Type C Phospholipases
Phosphatidylinositols
Adenylyl Cyclases
Complementary DNA
Chemical activation
Availability
Enzymes

ASJC Scopus subject areas

  • Pharmacology

Cite this

Regulatory GTP-binding proteins : Emerging concepts on their role in cell function. / Litosch, Irene.

In: Life Sciences, Vol. 41, No. 3, 20.07.1987, p. 251-258.

Research output: Contribution to journalArticle

@article{f23c897bf87d4c2bbdd6ec30792db9d5,
title = "Regulatory GTP-binding proteins: Emerging concepts on their role in cell function",
abstract = "The last few years have evidenced a tremendous expansion in our appreciation of the role of regulatory GTP-binding proteins in cellular activation. The availability of cholera and pertussis toxins to detect G proteins as well as methodological advances in the study of cellular function has afforded the opportunity to examine G protein participation in many cellular events. Regulation of adenylyl cyclase and cyclic GMP phosphodiesterase by G proteins has been demonstrated. Phosphatidylinositol-4,5-bisphosphate specific phospholipase C activity appears to be subject to G protein control. G proteins regulate inward K+ and Ca2+ channels through a mechanism which may be independent of effects on the above mentioned enzymes. Certainly, the number of G proteins which have been identified from sequencing of complementary DNA affords the potential for G protein involvement in many cellular events. Only three G proteins have however been isolated and functionally characterized, Gs, Gi and transducin. Whether all the functions of these proteins have been identified remains to be seen.",
author = "Irene Litosch",
year = "1987",
month = "7",
day = "20",
doi = "10.1016/0024-3205(87)90146-9",
language = "English",
volume = "41",
pages = "251--258",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Regulatory GTP-binding proteins

T2 - Emerging concepts on their role in cell function

AU - Litosch, Irene

PY - 1987/7/20

Y1 - 1987/7/20

N2 - The last few years have evidenced a tremendous expansion in our appreciation of the role of regulatory GTP-binding proteins in cellular activation. The availability of cholera and pertussis toxins to detect G proteins as well as methodological advances in the study of cellular function has afforded the opportunity to examine G protein participation in many cellular events. Regulation of adenylyl cyclase and cyclic GMP phosphodiesterase by G proteins has been demonstrated. Phosphatidylinositol-4,5-bisphosphate specific phospholipase C activity appears to be subject to G protein control. G proteins regulate inward K+ and Ca2+ channels through a mechanism which may be independent of effects on the above mentioned enzymes. Certainly, the number of G proteins which have been identified from sequencing of complementary DNA affords the potential for G protein involvement in many cellular events. Only three G proteins have however been isolated and functionally characterized, Gs, Gi and transducin. Whether all the functions of these proteins have been identified remains to be seen.

AB - The last few years have evidenced a tremendous expansion in our appreciation of the role of regulatory GTP-binding proteins in cellular activation. The availability of cholera and pertussis toxins to detect G proteins as well as methodological advances in the study of cellular function has afforded the opportunity to examine G protein participation in many cellular events. Regulation of adenylyl cyclase and cyclic GMP phosphodiesterase by G proteins has been demonstrated. Phosphatidylinositol-4,5-bisphosphate specific phospholipase C activity appears to be subject to G protein control. G proteins regulate inward K+ and Ca2+ channels through a mechanism which may be independent of effects on the above mentioned enzymes. Certainly, the number of G proteins which have been identified from sequencing of complementary DNA affords the potential for G protein involvement in many cellular events. Only three G proteins have however been isolated and functionally characterized, Gs, Gi and transducin. Whether all the functions of these proteins have been identified remains to be seen.

UR - http://www.scopus.com/inward/record.url?scp=0023259732&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023259732&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(87)90146-9

DO - 10.1016/0024-3205(87)90146-9

M3 - Article

C2 - 2439867

AN - SCOPUS:0023259732

VL - 41

SP - 251

EP - 258

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 3

ER -