Abstract
M1 muscarinic choligernic receptor, Gq and G11 (G q 11), and phospholipase C-β1 were highly purified from both natural sources and cells that express the appropriate cDNA's. When the proteins were co-reconstituted in into phospholipid vesicles, the receptor efficiently and selectively promoted the activation of if G q 11, leading to marked stimulation of PLC activity in the presence of GTPγS. No stimulation was observed in the presence of GTP, however, which led to the finding that PLC-β1 stimulates the hydrolysis of if G q 11-bound GTP at leasr 50-fold. Thus, PLC-β1 is a GTPase activating protein, a GAP, for its physiologic regulator G in q 11. We discuss the implications of PLC- β1's GAP activity on the M1 muscarinic cholinergic signaling pathway.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 413-419 |
| Number of pages | 7 |
| Journal | Life Sciences |
| Volume | 52 |
| Issue number | 5-6 |
| DOIs | |
| State | Published - 1993 |
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ASJC Scopus subject areas
- Pharmacology
Cite this
Regulation of the M1 muscarinic receptor-Gg-phospholipase C-β pathway by nucleotide exchange and GTP hydrolysis. / Ross, Elliott M.; Berstein, Gabriel.
In: Life Sciences, Vol. 52, No. 5-6, 1993, p. 413-419.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Regulation of the M1 muscarinic receptor-Gg-phospholipase C-β pathway by nucleotide exchange and GTP hydrolysis
AU - Ross, Elliott M.
AU - Berstein, Gabriel
PY - 1993
Y1 - 1993
N2 - M1 muscarinic choligernic receptor, Gq and G11 (G q 11), and phospholipase C-β1 were highly purified from both natural sources and cells that express the appropriate cDNA's. When the proteins were co-reconstituted in into phospholipid vesicles, the receptor efficiently and selectively promoted the activation of if G q 11, leading to marked stimulation of PLC activity in the presence of GTPγS. No stimulation was observed in the presence of GTP, however, which led to the finding that PLC-β1 stimulates the hydrolysis of if G q 11-bound GTP at leasr 50-fold. Thus, PLC-β1 is a GTPase activating protein, a GAP, for its physiologic regulator G in q 11. We discuss the implications of PLC- β1's GAP activity on the M1 muscarinic cholinergic signaling pathway.
AB - M1 muscarinic choligernic receptor, Gq and G11 (G q 11), and phospholipase C-β1 were highly purified from both natural sources and cells that express the appropriate cDNA's. When the proteins were co-reconstituted in into phospholipid vesicles, the receptor efficiently and selectively promoted the activation of if G q 11, leading to marked stimulation of PLC activity in the presence of GTPγS. No stimulation was observed in the presence of GTP, however, which led to the finding that PLC-β1 stimulates the hydrolysis of if G q 11-bound GTP at leasr 50-fold. Thus, PLC-β1 is a GTPase activating protein, a GAP, for its physiologic regulator G in q 11. We discuss the implications of PLC- β1's GAP activity on the M1 muscarinic cholinergic signaling pathway.
UR - http://www.scopus.com/inward/record.url?scp=0027446305&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027446305&partnerID=8YFLogxK
U2 - 10.1016/0024-3205(93)90296-F
DO - 10.1016/0024-3205(93)90296-F
M3 - Article
VL - 52
SP - 413
EP - 419
JO - Life Sciences
JF - Life Sciences
SN - 0024-3205
IS - 5-6
ER -