-
3
-
-
0023062991
-
G Proteins: Transducers of Receptor-Generated Signals
-
(1987)
Annu Rev Biochem
, vol.56
, pp. 615-649
-
-
Gilman1
-
4
-
-
0027495684
-
New Roles for G-Protein βγ-Dimers in Transmembrane Signalling
-
of special interest, This paper and [5⊎⊎] are recent reviews that recount the evolution of the function of G protein subunits in detail and with extensive references.
-
(1993)
Nature
, vol.365
, pp. 403-406
-
-
Clapham1
Neer2
-
5
-
-
0027253711
-
The importance of G-protein βλ subunits
-
of outstanding interest, This review proposes a model to explain the differences in sensitivity of various effectors to α- and βγ-subunits. Key elements are consideration of concentrations of different G proteins and the influence of GAP activities on the potential potency of α-subunits. See also [4⊎].
-
(1993)
Trends in Cell Biology
, vol.3
, pp. 230-236
-
-
Iňiguez-Lluhi1
Kleuss2
Gilman3
-
11
-
-
0026446880
-
Activation of Cytosolic Phosphoinositide Phospholipase C by G-Protein βγ-Subunits
-
(1992)
J Biol Chem
, vol.267
, pp. 23069-23075
-
-
Blank1
Brattain2
Exton3
-
12
-
-
0026676806
-
Isozyme-Selective Stimulation of Phospholipase C-β2 by G Protein βγ-Subunits
-
of special interest, PLCβ1 and PLCβ2 were expressed in COS cells, and extracts were examined for responses to βγ-subunits. PLCβ2 showed a much greater stimulation. The βγ-subunits of transducin were much less effective than βγ derived from brain.
-
(1992)
Nature
, vol.360
, pp. 684-686
-
-
Camps1
Carozzi2
Schnabel3
Scheer4
Parker5
Gierschik6
-
13
-
-
0026676807
-
Subunits βγ of Heterotrimetric G Protein Activate β2 Isoform of Phospholipase C
-
of special interest, The authors demonstrated stimulation of PLCβ2 activity when the enzyme was co-transfected with β- and γ-subunits in COS cells. PLCβ1 did not show this response. The importance of isoprenylation of the γ-subunit was suggested by failure of a mutant missing the site for prenylation to effect stimulation in this model.
-
(1992)
Nature
, vol.360
, pp. 686-689
-
-
Katz1
Wu2
Simon3
-
14
-
-
0026497034
-
βγ-Subunit Activation of G-Protein-Regulated Phospholipase C
-
11 purified from turkey erythrocytes.
-
(1992)
J Biol Chem
, vol.267
, pp. 25451-25456
-
-
Boyer1
Waldo2
Karden3
-
15
-
-
0027531123
-
Activation of Phosphatidylinositol Lipid-Specific Phospholipase C-β3 by G-Protein βγ-Subunits
-
of special interest, This report demonstrates that a purified PLCβ3 isoform is also activated by βγ-subunits. As in [14⊎], a direct action of βγ on the PLC is demonstrated.
-
(1993)
FEBS Lett
, vol.315
, pp. 340-342
-
-
Carozzi1
Camps2
Gierschik3
Parker4
-
16
-
-
0027214868
-
Regulation of Purified Subtypes of Phosphatidylinositol Specific Phospholipase C β by G protein α and β/γ-Subunits
-
q, and the order of response was different in this direct comparison of subunits.
-
(1993)
J Biol Chem
, vol.268
, pp. 9667-9674
-
-
Smrcka1
Sternweis2
-
17
-
-
0027418803
-
Activation of Phospholipase C Isozymes by G Protein βγ-Subunits
-
of outstanding interest, This report compared three purified isoforms of PLC and demonstrated an order of response: PLCβ3 〉 PLCβ2 〉 PLCβ1. The authors also reported a small twofold stimulation of PLCδ1 by purified βγ, but no activation of PLCγ1.
-
(1993)
J Biol Chem
, vol.268
, pp. 4573-4576
-
-
Park1
Jhon2
Lee3
Lee4
Goo Rhee5
-
19
-
-
0027362142
-
A G-Protein-Coupled 130 kDa Phospholipase C Isozyme, PLCβ4, from the Particulate Fraction of Bovine Cerebellum
-
(1993)
FEBS Lett
, vol.331
, pp. 38-42
-
-
Min1
Kim2
Lee3
Suh4
Ryu5
-
20
-
-
0027537482
-
Removal of the Carboxyl-Terminal Region of Phospholipase C-β1 by Calpain Abolishes Activation by Gαq
-
q.
-
(1993)
J Biol Chem
, vol.268
, pp. 3710-3714
-
-
Park1
Jhon2
Lee3
Ryu4
Rhee5
-
21
-
-
0027178468
-
Activation of Phospholipase C β2 by the α and βγ-Subunits of Trimeric GTP-Binding Protein
-
16-subunits
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 5297-5301
-
-
Wu1
Katz2
Simon3
-
23
-
-
0026785920
-
Adenylyl Cyclases
-
of special interest, This brief review and references therein present a picture of the earlier work on adenylyl cyclase subtypes.
-
(1992)
Cell
, vol.70
, pp. 869-872
-
-
Tang1
Gilman2
-
25
-
-
0027458559
-
Regulation of Purified Type I and Type II Adenylylcyclases by G Protein βγ-Subunits
-
of special interest, The authors of this brief report used purified recombinant adenylyl cyclase to demonstrate that the respective inhibitory or stimulatory effects of βγ-subunits on the type 1 and type 2 isozymes occurs through direct action on the enzymes.
-
(1993)
J Biol Chem
, vol.268
, pp. 9-12
-
-
Taussig1
Quarmby2
Gilman3
-
27
-
-
0028133063
-
Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases.
-
i were shown to be equally efficacious. Extensive characterization of four cyclase subtypes is reported. Experiments with combinations of subunits suggest that the binding sites for α- and βγ-subunits are independent.
-
(1994)
J Biol Chem
-
-
Taussig1
Tang2
Hepler3
Gilman4
-
28
-
-
0026752495
-
Different β-Subunits Determine G-Protein Interaction with Transmembrane Receptors
-
2+ currents by muscarinic and somatostatin receptors, respectively.
-
(1992)
Nature
, vol.358
, pp. 424-426
-
-
Kleuss1
Scherubl2
Heschler3
Schultz4
Wittig5
-
29
-
-
0027530916
-
Selectivity in Signal Transduction Determined by γ-Subunits of Heterotrimeric G Proteins
-
2+ currents by somatostatin and muscarinic receptors, respectively.
-
(1993)
Science
, vol.259
, pp. 832-834
-
-
Kleuss1
Scherübl2
Hescheler3
Schultz4
Wittig5
-
30
-
-
0026452219
-
G protein beta gamma subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of gamma.
-
1 constructs did not yield a functional dimer.
-
(1992)
J Biol Chem
, vol.267
, pp. 23409-23417
-
-
Iñiguez-Lluhi1
Simon2
Robishaw3
Gilman4
-
31
-
-
0028169730
-
G Protein βγ-Subunits: Simplified Purification and Properties of Novel Isoforms
-
1). Expressed βγ containing a γ-subunit mutated in the cysteine required for isoprenylation was examined; although βγ complexes were formed with the non-prenylated protein, such complexes were deficient in interaction with α-subunits and were ineffective on adenylyl cyclase.
-
(1994)
J Biol Chem
-
-
Ueda1
Iñiguez-Lluhi2
Lee3
Smrcka4
Robishaw5
Gilman6
-
32
-
-
0026655036
-
Specificity of G Protein β and γ-Subunit Interactions
-
2. This paper and [30⊎] indicate that some combinations of subunits are not formed or are not stable.
-
(1992)
J Biol Chem
, vol.267
, pp. 13807-13810
-
-
Schmidt1
Thomas2
Levine3
Neer4
-
35
-
-
0027198334
-
Guanine Nucleotide-Specific Phosphate Transfer by Guanine Nucleotide-Specific Phosphate Transfer by Guanine Nucleotide-Binding Regulatory Protein β-Subunits
-
of special interest, The manuscript extends the observations of [34] to show that β-subunits other than transducin β can be phosphorylated in a GTP-dependent fashion. This appears to occur via GTP bound to α-subunits: the phosphate on the β-subunits can be transferred back onto GDP bound to α-subunits. Evidence suggests that a histidine residue on β is the site of phosphorylation, and that the modification is short-lived.
-
(1993)
J Biol Chem
, vol.268
, pp. 18111-18118
-
-
Wieland1
Nürnberg2
Ulibarri3
Kaldenberg-Stasch4
Schultz5
Jakobs6
-
36
-
-
0025315797
-
Dual Regulation by G Proteins of Agonist-Dependent Phosphorylation of Muscarinic Acetylcholine Receptors
-
(1990)
FEBS Lett
, vol.268
, pp. 43-47
-
-
Haga1
Haga2
-
37
-
-
0026793617
-
Activation by G Protein βγ-Subunits of Agonist- or Light-Dependent Phosphorylation of Muscarinic Acetylcholine Receptors and Rhodopsin
-
of special interest, Studies reported in [36] with the muscarinic receptor were extended to rhodopsin. Thus, βγ-subunits derived from several G proteins were shown to facilitate light-dependent phosphorylation of rhodopsin with a receptor kinase that behaves like the β-receptor kinase. Phosphorylation of rhodopsin by rhodopsin kinase was not stimulated by βγ.
-
(1992)
J Biol Chem
, vol.267
, pp. 2222-2227
-
-
Haga1
Haga2
-
38
-
-
0026803164
-
Role of βγ-Subunits of G Proteins in Targeting the β-Adrenergic Receptor Kinase to Membrane-Bound Receptors
-
of special interest, The action of purified βARK on both β-adrenergic receptors and rhodopsin was stimulated by βγ-subunits. The authors present evidence that the βγ-subunits did not affect the intrinsic activity of βARK on a peptide substrate but did promote localization of the kinase into particulate fractions.
-
(1992)
Science
, vol.257
, pp. 1264-1267
-
-
Pitcher1
Inglese2
Higgins3
Arriza4
Casey5
Kim6
Benovic7
Kwatra8
Caron9
Lefkowitz10
-
39
-
-
0026726050
-
Isoprenylation in Regulation of Signal Transduction by G-Protein-Coupled Receptor Kinases
-
of special interest, The authors reported that rhodopsin kinase was not stimulated by βγ-subunits. Addition of the carboxyl isoprenylation sequence of rhodopsin kinase onto βARK increased localization of the βARK to particulate fractions and increased its activity in the absence of βγ. The authors ascribe the role of βγ to membrane localization.
-
(1992)
Nature
, vol.359
, pp. 147-150
-
-
Inglese1
Koch2
Caron3
Lefkowitz4
-
40
-
-
0027185782
-
Mechanism of β-Adrenergic Receptor Kinase Activation by G Proteins
-
of outstanding interest, The authors used phospholipid vesicles with incorporated receptors and G protein subunits to measure direct binding of purified βARK. While association was observed with both βγ-subunits and the heterotrimeric G protein, the best binding of the kinase was observed in the presence of both activated β2-adrenergic receptors and βγ-subunits. The authors further report that the combination of βγ and receptor caused synergistic activation of the kinase activity using a peptide substrate.
-
(1993)
J Biol Chem
, vol.268
, pp. 15412-15418
-
-
Kim1
Dion2
Benovic3
-
41
-
-
0026716049
-
Phosducin is a Protein Kinase A-Regulated G-Protein Regulator
-
of special interest, Recombinant phosducin was shown to inhibit the GTPase activity and enhance the binding of GTPγS to various purified G proteins. Phosphorylation of the phosducin with protein kinase A attenuated these activities and the inhibitory effects of phosducin on β-adrenergic stimulation of adenylyl cyclase activity.
-
(1992)
Nature
, vol.358
, pp. 73-76
-
-
Bauer1
Müller2
Puzicha3
Pippig4
Obermaier5
-
42
-
-
0026453108
-
Regulation of Retinal cGMP Cascade by Phosducin in Bovine Rod Photoreceptor Cells
-
1 and cGMP-phosphodiesterase in rod outer segments. This effect could be reversed by adding excess βγ. The authors also present data to indicate that the phosducin probably interacts with βγ that is free of transducin α, in that phosducin did not elute βγ-subunits from non-activated membranes or inhibit initial activation of transducin by rhodopsin.
-
(1992)
J Biol Chem
, vol.267
, pp. 25104-25112
-
-
Lee1
Ting2
Lieberman3
Tobias4
Lolley5
Ho6
-
43
-
-
0027048684
-
The Protein Kinase Homologue Ste20p is Required to Link the Yeast Pheromone Response G-Protein βγ-Subunits to Downstream Signalling Components
-
of outstanding interest, The authors identified a new gene, STE20, in the yeast Saccharomyces cerevisiae, that encodes an apparent protein kinase whose expression can overcome the mating defect of a strain expressing a dominant negative βγ. This suggests an interaction between the two components and potentially, a direct regulatory relationship.
-
(1992)
EMBO J
, vol.11
, pp. 4815-4824
-
-
Leberer1
Dignard2
Harcus3
Thomas4
Whiteway5
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