Abstract
The biochemical properties of three stimulatory guanine nucleotide-binding protein (G-protein) a subunits, the large and small forms of Gs, Gs-l (52 kDa) and Gs-8 (45 kDa), and the olfactory specific G-protein, Golf, have been compared. Complementary DNAs (cDNAs) encoding each α subunit were independently expressed in a mammalian cell line deficient in endogenous stimulatory G-proteins (S49 cyc-kin-). Gs-l and Gs-8 respond similarly to activation by the β-adrenergic agonist isoproterenol (EC50 = 80 and 60 nM, respectively) and the receptor-independent G-protein activators guanosine 5-O-3-(thio)triphosphate) (GTPγS) and AlF4-. The ability of Golf to interact with the β-adrenergic receptor was also examined. Surprisingly, Golf interacts with β-adrenergic receptors and is activated by isoproterenol (EC50 = 120 nM). All three G-proteins respond similarly to treatment with different α, β, and γ thiophosphoryl analogs of GTP. Specifically, (R)-GTPαS and GTPγS activate each G-protein, whereas (S)-GTPαS and (R)-or (S)-GTPβS are inactive. In addition, similar to Gsα, Golfα is covalently modified and constitutively activated by cholera toxin. These studies demonstrate that all three stimulatory G-proteins are functionally and structurally similar, however, subtle differences between Golf and the two forms of Gs appear to modulate their interactions with receptors.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2671-2676 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 265 |
| Issue number | 5 |
| State | Published - 1990 |
Fingerprint
ASJC Scopus subject areas
- Biochemistry
Cite this
Biochemical characterization of three stimulatory GTP-binding proteins : The large and small forms of Gs and the olfactory-specific G-protein, Golf. / Jones, David T.; Masters, Susan B.; Bourne, Henry R.; Reed, Randall R.
In: Journal of Biological Chemistry, Vol. 265, No. 5, 1990, p. 2671-2676.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biochemical characterization of three stimulatory GTP-binding proteins
T2 - The large and small forms of Gs and the olfactory-specific G-protein, Golf
AU - Jones, David T.
AU - Masters, Susan B.
AU - Bourne, Henry R.
AU - Reed, Randall R
PY - 1990
Y1 - 1990
N2 - The biochemical properties of three stimulatory guanine nucleotide-binding protein (G-protein) a subunits, the large and small forms of Gs, Gs-l (52 kDa) and Gs-8 (45 kDa), and the olfactory specific G-protein, Golf, have been compared. Complementary DNAs (cDNAs) encoding each α subunit were independently expressed in a mammalian cell line deficient in endogenous stimulatory G-proteins (S49 cyc-kin-). Gs-l and Gs-8 respond similarly to activation by the β-adrenergic agonist isoproterenol (EC50 = 80 and 60 nM, respectively) and the receptor-independent G-protein activators guanosine 5-O-3-(thio)triphosphate) (GTPγS) and AlF4-. The ability of Golf to interact with the β-adrenergic receptor was also examined. Surprisingly, Golf interacts with β-adrenergic receptors and is activated by isoproterenol (EC50 = 120 nM). All three G-proteins respond similarly to treatment with different α, β, and γ thiophosphoryl analogs of GTP. Specifically, (R)-GTPαS and GTPγS activate each G-protein, whereas (S)-GTPαS and (R)-or (S)-GTPβS are inactive. In addition, similar to Gsα, Golfα is covalently modified and constitutively activated by cholera toxin. These studies demonstrate that all three stimulatory G-proteins are functionally and structurally similar, however, subtle differences between Golf and the two forms of Gs appear to modulate their interactions with receptors.
AB - The biochemical properties of three stimulatory guanine nucleotide-binding protein (G-protein) a subunits, the large and small forms of Gs, Gs-l (52 kDa) and Gs-8 (45 kDa), and the olfactory specific G-protein, Golf, have been compared. Complementary DNAs (cDNAs) encoding each α subunit were independently expressed in a mammalian cell line deficient in endogenous stimulatory G-proteins (S49 cyc-kin-). Gs-l and Gs-8 respond similarly to activation by the β-adrenergic agonist isoproterenol (EC50 = 80 and 60 nM, respectively) and the receptor-independent G-protein activators guanosine 5-O-3-(thio)triphosphate) (GTPγS) and AlF4-. The ability of Golf to interact with the β-adrenergic receptor was also examined. Surprisingly, Golf interacts with β-adrenergic receptors and is activated by isoproterenol (EC50 = 120 nM). All three G-proteins respond similarly to treatment with different α, β, and γ thiophosphoryl analogs of GTP. Specifically, (R)-GTPαS and GTPγS activate each G-protein, whereas (S)-GTPαS and (R)-or (S)-GTPβS are inactive. In addition, similar to Gsα, Golfα is covalently modified and constitutively activated by cholera toxin. These studies demonstrate that all three stimulatory G-proteins are functionally and structurally similar, however, subtle differences between Golf and the two forms of Gs appear to modulate their interactions with receptors.
UR - http://www.scopus.com/inward/record.url?scp=0025347087&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025347087&partnerID=8YFLogxK
M3 - Article
C2 - 2105931
AN - SCOPUS:0025347087
VL - 265
SP - 2671
EP - 2676
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 5
ER -