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 language | English |
|---|---|
| Pages (from-to) | 251-258 |
| Number of pages | 8 |
| Journal | Life Sciences |
| Volume | 41 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 20 1987 |
| Externally published | Yes |
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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 journal › Article
}
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 -