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Science 22 May 1998:
Vol. 280. no. 5367, pp. 1271 - 1274
DOI: 10.1126/science.280.5367.1271
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Reports
Molecular Basis for Interactions of G Protein   Subunits with Effectors
Carolyn E. Ford,
*
Nikolai P. Skiba,
*
Hyunsu Bae,
Yehia Daaka,
Eitan Reuveny,
Lee R. Shekter,
Ramon Rosal,
Gezhi Weng,
Chii-Shen Yang,
Ravi Iyengar,
Richard J. Miller,
Lily Y. Jan,
Robert J. Lefkowitz,
Heidi E. Hamm
Both the  and   subunits of heterotrimeric guanine
nucleotide-binding proteins (G proteins) communicate
signals from receptors to effectors. G subunits can regulate a
diverse array of effectors, including ion channels and enzymes. G
subunits bound to guanine diphosphate (G-GDP) inhibit signal
transduction through G subunits, suggesting a common interface on
G subunits for G binding and effector interaction. The
molecular basis for interaction of G with effectors was
characterized by mutational analysis of G residues that make contact
with G-GDP. Analysis of the ability of these mutants to regulate the
activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-2, and -adrenergic receptor kinase revealed the
G residues required for activation of each effector and provides
evidence for partially overlapping domains on G for regulation of
these effectors. This organization of interaction regions on G for
different effectors and G explains why subunit dissociation is
crucial for signal transmission through G subunits.
C. E. Ford, N. P. Skiba, H. Bae, C.-S. Yang, H. E. Hamm, Institute for Neuroscience and Department of Molecular
Pharmacology and Biological Chemistry, Northwestern University,
Chicago, IL 60611, USA.
Y. Daaka and R. J. Lefkowitz, Howard Hughes Medical Institute and
Department of Medicine, Duke University Medical Center, Durham, NC
27710, USA.
E. Reuveny, Department of Membrane Research and Biophysics, Weizmann
Institute of Science, Rehovot 76100, Israel.
L. R. Shekter and R. J. Miller, Department of Pharmacological
and Physiological Sciences, University of Chicago, Chicago, IL 60637, USA.
R. Rosal, G. Weng, R. Iyengar, Department of Pharmacology, Mount Sinai
School of Medicine, New York, NY 10029, USA.
L. Y. Jan, Howard Hughes Medical Institute and Department of
Physiology and Biochemistry, University of California at San Francisco,
San Francisco, CA 94143, USA.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
h-hamm{at}nwu.edu
Upon receptor activation, G
proteins dissociate into free G and G subunits that can
activate various effectors (1). Effector proteins of the
G complex include phospholipases (2), adenylyl
cyclases (3), ion channels (4), G
protein-coupled receptor kinases (5) and
phosphoinositide 3-kinases (6). Other potential G
effectors include dynamin I and the nonreceptor protein tyrosine
kinases Btk and Tsk (7). GDP-bound G subunits (G-GDP)
can compete with G effectors and deactivate G-dependent signaling, suggesting that G may use a common binding surface for
interaction with G and with its diverse effectors. Two regions on
G that interact with G have been defined by the crystal structures of heterotrimeric G (8), the switch
interface (G residues 57, 59, 98, 99, 101, 117, 119, 143, 186, 228, and 332) and the NH2-terminal interface (G residues 55, 78, 80 and 89). Each of these residues on retinal G (G1) was
substituted with alanine, and each G1 mutant was expressed with
either G1 or G2, two isoforms of the G subunit. All
mutated G11 dimers were folded properly, were
post-translationally modified appropriately, and were expressed at
similar amounts as in the wild type (9). The G mutants
were tested for their ability to assemble into heterotrimers with G,
to be activated by rhodopsin, and to interact with G
downstream signaling partners: -adrenergic receptor kinase (ARK),
phospholipase C-2 (PLC-2), adenylyl cyclase 2 (AC2), muscarinic
potassium channel (GIRK1/GIRK4), and the calcium channel 1B subunit
(CC1B).
To determine whether purified G1H61
mutants could form heterotrimers, we measured the ability of the
G mutants to facilitate pertussis toxin-catalyzed
adenosine diphosphate (ADP) ribosylation of transducin G-GDP (Gt)
(10). All mutants could support some level of ADP
ribosylation, although G mutants Ile80  Ala80 (I80A), K89A, L117A, and W332A (11) showed
reduced ability to form heterotrimers (Fig.
1A).
Fig. 1.
Effects of G1H61
on heterotrimer assembly and receptor interaction. The data are the
normalized percentage of wild-type (WT)
recombinant G activity. (A) The ability of
recombinant G1H61 and G1 mutants to assemble into
heterotrimers with Gt was determined by testing whether pertussis
toxin could ADP-ribosylate Gt with [32P]nicotinamide
adenine dinucleotide (10). The G residue mutated to
alanine is indicated by a number beneath each bar in the figure. Clear
bar (C) represents the basal amount of ADP-ribosylation of Gt that
occurred in absence of G. (B) The ability of
recombinant G1H61 and G1 mutants to bind Gt and
interact with rhodopsin was determined by the amount of
[35S]GTP--S binding catalyzed by light-activated
rhodopsin (12). Clear bar (C) is the basal amount of
[35S]GTP--S binding to Gt in the presence of
urea-washed rod outer segment membranes (50 nM) without added G.
The data represent the mean ± SEM of duplicate determinations in
three independent experiments. Alanine mutants that have a
distinguishable activity from the wild type are indicated by gray bars;
those with activity similar to the wild type are indicated by black
bars (11).
[View Larger Version of this Image (26K GIF file)]
Because G is essential for functional heterotrimer
interaction with activated receptors that catalyze the exchange of GDP for guanosine triphosphate (GTP) on the G subunit, we also measured the ability of the G mutants to support light-activated
rhodopsin-catalyzed nucleotide exchange on the subunit of
transducin (Gt) (12). All switch interface mutants
(except K57A and Y59A) and the NH2-terminal interface
mutants I80A and K89A were defective in formation of functional
heterotrimers (Fig. 1B). Some G mutants were impaired in both
assays, indicating that residues 80, 89, 117, and 332 of G are the
major determinants of binding to Gt. The switch interface mutants
(S98A, W99A, M101A, N143A, and D186A) were normal in heterotrimer
assembly, but were impaired functionally in supporting receptor-catalyzed nucleotide exchange on Gt. This observation indicates that G may actively participate in receptor-catalyzed nucleotide exchange, rather than being simply a passive binding partner
in receptor-G protein interactions.
G mediates translocation of G protein-coupled receptor
kinases from the cytosol to the membrane, in order that these kinases can phosphorylate activated G protein-coupled receptors and
initiate receptor internalization (13). The G mutants
varied in their ability to associate with ARK1 (Fig.
2A) (14). Alanine mutations at
G residues 117 and 143 resulted in decreased binding to ARK1. In
contrast, alanine mutations at G residues 57, 59, 89, 186, and 332 of G led to increased binding to ARK1. The mutations that
resulted in decreased binding are found on the left side of the G
surface (Fig. 3) and likely form the
ARK binding interface, whereas those mutations that led to increased
binding were clustered together at the middle of the structure (G
residues 57, 59, and 332) or are at the right side of the surface (G
residue 89).
Fig. 2.
G-dependent
interactions with ARK, PLC-2, AC2, muscarinic potassium channel,
and CC1B-containing calcium channel. (A) The amount of
G1 present in ARK immune complexes was detected as described
(14). Light orange bars show those mutations that decrease
G/ARK interaction, while dark orange bars show mutations that
increase the interaction. The data contained in the bar graph represent
duplicate determinations in two independent experiments. (B) G11-dependent activation of PLC-2 was
determined as described (17). Clear bar (C) represents the
basal PLC-2 activity in the absence of G. Light purple bars
show those mutations that decrease G-mediated PLC2 activation,
while dark purple bars indicate mutations that determine enhanced
activation. The data are presented as the normalized percentage of
wild-type recombinant G activity and represent the mean ± SEM of duplicate determinations in three independent experiments.
(C) G12-dependent activation of AC2 was determined by
reconstituting membranes as described (18). Data represent
duplicate determinations from two independent experiments.
(D) G12-dependent activation of GIRK potassium channel was determined as described (19). Protein
immunoblotting showed that all mutants were expressed in equal amounts.
Clear bar (C) represents control oocytes injected with GIRK1, GIRK4, and G2 RNAs. (E) G12-dependent inhibition of
CC1B calcium channels was determined as described (21).
Protein immunoblotting revealed that all mutants were expressed in
similar amounts. The amount of G-dependent inhibition was
calculated as a ratio of the mean prepulse facilitation (MPF) in either
the absence or presence of G. MPF is the statistically averaged
relief of the channel inhibition by use of a large depolarizing
prepulse. Clear bar (C) represents channel activity in absence of
G. The light yellow bars indicate the G1 mutations that
decrease channel modulation and lead to calcium currents that are
statistically indistinguishable from the basal calcium current
(P < 0.1 for K78A and W332A mutants and P < 0.01 for M101A, N119A, T143A, and D186A mutants). The dark yellow bars
indicate G1 mutants that have increased inhibitory activity
(P < 0.001 for L55A mutant and P < 0.01 for
I80A mutant).
[View Larger Version of this Image (26K GIF file)]
Fig. 3.
A schematic representation of the regions of
G involved in interactions with effectors and G subunit. The
crystal coordinates of G11 [Protein Databank entry 1tbg;
(8, 26)] were used to generate a surface model of the
dimer in GRASP. G is gray, and G is pink. The pale green surface
is the area on G that is covered by G in the G protein
heterotrimer crystal structure. The effector-interacting residues on
G are circled with a different color for each effector: orange,
ARK; magenta, PLC-2; teal, AC2; blue, potassium channel; and
yellow, calcium channel. G-GDP, when bound to G, covers all
these distinct yet partially overlapping effector interaction regions
on G and, thus, blocks G regulation of all the effectors. This
figure and other more detailed figures showing residues interacting
with individual effectors can be viewed at
http://www.sciencemag.org/feature/data/976104.shl
[View Larger Version of this Image (79K GIF file)]
G is an important modulator of various isoforms of
phospholipase C- (2, 15) and adenylyl cyclase
(16), effectors that regulate intracellular concentration of
second messengers inositol 1,4,5-triphosphate and cyclic adenosine
3',5'-monophosphate. The ability of the G mutants to stimulate
the activity of PLC-2 was determined by quantitating the amount of
inositol 1,4,5-triphosphate produced by the purified enzyme in the
presence of the G mutants (17). Some 13 of the 15 G-interacting residues of G we tested were important for
G-dependent activation of PLC-2, suggesting that G and
PLC- binding regions on G are overlapping (Fig. 2B). Mutants W99A
and D228A no longer activated PLC-2 and mutants I80A, K89A, M101A,
L117A, N119A, T143A, D186A, and W332A were less effective than
wild-type G. Mutants L55A and S98A activated PLC-2 to a
greater extent than wild-type G. These residues are circled in
magenta on the G surface (Fig. 3). The effects of the G
mutants on AC2 activation were determined in vitro (18) in
the presence of constitutively activated Gs that has glutamine at
residue 227 mutated to leucine (Q227L). All the Ala mutations of G
residues, except I80A and T143A, had decreased ability to activate AC2
(Fig. 2C); their locations on the G structure are indicated in
teal (Fig. 3).
We also measured K+ currents in Xenopus laevis
oocytes injected with RNAs for GIRK1/GIRK4 and G mutants
(19). The ability of G to increase conductance through
the muscarinic potassium channel GIRK1/GIRK4 was disrupted by alanine
mutations at G residues 55, 78, 80, 89, 99, and 228 (Fig. 2D). All
these G residues except W99 and D228 cluster within the
NH2-terminal interface of G (Fig. 3; blue lines).
G inhibits the activity of certain calcium channels
(20). We measured the ability of G mutants to inhibit
the conductance of Ca2+ channels in HEK 293 cells
expressing CC1B-containing Ca2+ channels and G
mutants (21). Alanine mutations of G residues 55 and 80, which lie close together at the top of G, had enhanced ability to
inhibit current through CC1B-containing Ca2+ channels
(Fig. 2E). Alanine mutations of G residues 78, 101, 119, 143, 186, and 332 were no longer able to inhibit current through calcium
channels.
Our results demonstrate that many of the G-interacting residues
of G are important in interactions between G and its signaling partners, and show the functional importance of individual amino acids
in the signal transfer from G to effector activation. Alanine
mutation of these G residues may increase, decrease, or abolish
G-dependent interactions. It was unexpected to find G
mutants that are better than the wild type at stimulating the activity
of PLC-2 and inhibiting Ca2+ channels. One possible
reason for such "gain-of-function" mutations is that turn-off of
G-mediated signaling requires G-GDP competition with
effectors. The normal side chains at these positions may be
destabilizing to effector interaction resulting in a lower affinity in
order to allow reassembly of heterotrimeric G.
Each signaling partner for G relies on a different subset of G
residues for its interaction and hence, creates a set of unique
"footprints" on G (Fig. 3). These results are consistent with
studies that have suggested a common effector binding surface on
G located near the region of residues 70 to 145 of G
(22). These data raise an interesting issue of how G
proteins and their effectors are oriented with respect to the membrane
and whether their orientations change during subunit dissociation and
activation (8, 23). The G-binding surface on G may
not be the only region of effector interaction. Other G regions
of effector interactions that have been implicated are the coiled-coil
interface at the NH2-termini of G and G
(24) and the COOH-terminal region of G (25).
The alanine mutations of G-interacting G residues provide an
initial framework to determine how G subunits interact with and
regulate so many different effectors that have so little structural similarity. Our studies show that the effector interaction regions are
clustered on G such that they partially overlap one another (Fig.
3). This mode of clustering allows for one key regulator (G) to
regulate G signal transmission to multiple effectors.
REFERENCES AND NOTES
-
H. E. Hamm,
J. Biol. Chem.
273,
669
(1998)
[Free Full Text]
;
E. J. Neer,
Cell
80,
249
(1995)
[CrossRef] [Web of Science] [Medline]
;
D. E. Clapham and
E. J. Neer,
Annu. Rev. Pharmacol. Toxicol.
37,
167
(1997)
[CrossRef] [Web of Science] [Medline]
.
-
S. G. Rhee and
Y. S. Bae,
J. Biol. Chem.
272,
15045
(1997)
[Free Full Text]
.
-
R. K. Sunahara,
C. W. Dessauer,
A. G. Gilman,
Annu. Rev. Pharmacol. Toxicol.
36,
461
(1996)
[CrossRef] [Web of Science] [Medline]
.
-
T. Schneider,
P. Igelmund,
T. Hescheler,
Trends Pharmacol. Sci.
18,
8
(1997)
[CrossRef] [Medline]
.
-
J. A. Pitcher,
et al.,
Science
257,
1264
(1992)
[Abstract/Free Full Text]
;
N. J. Freedman and
R. J. Lefkowitz,
Recent Prog. Horm. Res.
51,
319
(1996)
.
-
B. Vanhaesebroeck,
S. J. Leevers,
G. Panayotou,
M. D. Waterfield,
Trends Biochem. Sci.
22,
267
(1997)
[CrossRef] [Web of Science] [Medline]
.
-
H. C. Lin and
A. G. Gilman,
J. Biol. Chem.
271,
27979
(1996)
[Abstract/Free Full Text]
;
S. A. Langhans-Rajasekaran,
Y. Wan,
X. Y. Huang,
Proc. Natl. Acad. Sci. U.S.A.
92,
8601
(1995)
[Abstract/Free Full Text]
.
-
D. G. Lambright,
et al.,
Nature
379,
311
(1996)
[CrossRef] [Medline]
;
M. A. Wall,
et al.,
Cell
83,
1047
(1995)
[CrossRef] [Web of Science] [Medline]
.
-
Cloning of hexahistidine-tagged G1 (H6G1),
generation of the G1 and H6G1 recombinant
baculoviruses, detailed protocols for recombinant protein expression in
Sf9 insect cells, and detailed protocols for purification of G
complexes are described at
http://www.sciencemag.org/feature/data/976104.shl#9. The recombinant
wild-type G was equivalent to native G in the assays used
in our study. All mutated G1 subunits assembled properly with
H6G1 subunits as judged by the trypsin protection assay.
We determined, with mass spectrometry, that the recombinant G
dimers tested were properly modified by isoprenylation and carboxymethylation.
-
The pertussis toxin-catalyzed ADP ribosylation assay
was done essentially as described [
T. Katada,
et al.,
Methods Enzymol.
237,
131
(1994)
[Web of Science] [Medline]
]. Details
of modifications are provided at
http://www.sciencemag.org/feature/data/976104.shl#10.
-
Single-letter abbreviations for the amino acid residues are as
follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I,
Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T,
Thr; V, Val; W, Trp; and Y, Tyr.
-
Rhodopsin-catalyzed [35S]GTP--S binding assay
was done essentially as described [
N. P. Skiba,
et al.,
J. Biol. Chem.
271,
413
(1996)
[Abstract/Free Full Text]
]. Details of modifications are described at
http://www.sciencemag.org/feature/data/976104.shl#12.
-
R. H. Stoffel,
J. A. Pitcher,
R. J. Lefkowitz,
J. Membr. Biol.
157,
1
(1997)
[CrossRef] [Web of Science] [Medline]
.
-
COS-7 cells were transiently transfected with either G1 or
G1 mutant, G2, and ARK1 cDNAs (2 µg). The amount of G1
associated with ARK was determined as described [
Y. Daaka ,
et al.,
Proc. Natl. Acad. Sci. U.S.A.
94,
2180
(1997)
[Abstract/Free Full Text]
.
-
M. Camps,
et al.,
Nature
360,
684
(1992)
[CrossRef] [Medline]
; A. Katz, D. Wu, M. I. Simon, ibid., p. 686.
-
W.-J. Tang and
A. G. Gilman,
Science
254,
1500
(1991)
[Abstract/Free Full Text]
.
-
M. De Vivo,
Methods Enzymol.
238,
131
(1994)
[Web of Science] [Medline]
;
V. Romoser,
R. V. Ball,
A. Smrcka,
J. Biol. Chem.
271,
25071
(1996)
[Abstract/Free Full Text]
. G11-dependent activation of
PLC-2 was determined by reconstitution of purified
H6PLC-2, G or mutants, and radiolabeled
phosphatidylinositol 4,5-diphosphate in a mixed detergent-phospholipid
micelle. See http://www.sciencemag.org/feature/data/976104.shl#17 for
details of PLC-2 expression, purification, and activation assay.
-
J. Chen,
et al.,
Science
268,
1166
(1995)
[Abstract/Free Full Text]
. In the presence of 0.14% CHAPS detergent, insect cell
membranes that expressed recombinant AC2 were mixed with purified
constitutively active Q227L-Gs and insect cells membranes expressing
both recombinant H6G2 and either recombinant wild-type
or mutant G1. Details of the assay are described at
http://www.sciencemag.org/feature/data/976104.shl#18.
-
E. Reuveny,
et al.,
Nature
370,
143
(1994)
[CrossRef] [Medline]
;
C.-L. Huang,
P. A. Slesinger,
P.
J. Casey,
Y. N. Jan,
L. Y. Jan,
Neuron
15,
1133
(1995)
[CrossRef] [Web of Science] [Medline]
. RNAs for either G1 or G1 mutants, G2,
GIRK1, and GIRK4 were injected into Xenopus oocytes,
and the K+ current was measured by voltage clamp after 3 to
5 days. For details, see
http://www.sciencemag.org/feature/data/976104.shl#19.
-
S. R. Ikeda,
Nature
380,
255
(1996)
[CrossRef] [Medline]
; S. Herlitze et al., ibid., p. 258.
-
L. R. Shekter,
R. Taussig,
S. E. Gillard,
R. J. Miller,
Mol. Pharmacol.
52,
282
(1997)
[Abstract/Free Full Text]
. The
Ca2+-current was measured by the whole-cell patch clamp
technique in HEK-293 cells stably expressing the calcium channel
CC1B subunit and ancilliary calcium channel subunits (1 and
2B
 ) and transiently expressing cDNAs encoding G1 (or mutants)
and G2. Refer to http://www.sciencemag.org/feature/data/976104.shl#21 for details.
-
G. Weng,
et al.,
J. Biol. Chem.
271,
26445
(1996)
[Abstract/Free Full Text]
;
Y. Chen,
et al.,
Proc. Natl. Acad. Sci. U.S.A.
94,
2711
(1997)
[Abstract/Free Full Text]
;
K. Yan and
N. Gautam,
J. Biol. Chem.
271,
17597
(1996)
[Abstract/Free Full Text]
; ibid., 272, 2056 (1997).
-
J. J. G. Tesmer,
R. K. Sunahara,
A. G. Gilman,
S. R. Sprang,
Science
278,
1907
(1997)
[Abstract/Free Full Text]
.
-
E. Leberer,
D. Dignard,
L. Hougan,
D. Y. Thomas,
M. Whiteway,
EMBO J.
11,
4805
(1992)
[Web of Science] [Medline]
;
A. V. Grishin,
J. L. Weiner,
K. J. Blumer,
Mol. Cell. Biol.
14,
4571
(1994)
[Abstract/Free Full Text]
;
S. Pellegrino,
S. Zhang,
A. Garritsen,
W. F. Simonds,
J. Biol. Chem.
272,
25360
(1997)
[Abstract/Free Full Text]
.
-
S. Zhang,
O. A. Coso,
R. Collins,
J. S. Gutkind,
W. F. Simonds,
J. Biol. Chem.
271,
20208
(1996)
[Abstract/Free Full Text]
;
K. Blüml,
et al.,
EMBO J.
16,
4908
(1997)
[CrossRef] [Web of Science] [Medline]
;
J. Yamauchi,
Y. Kaziro,
H. Itoh,
J. Biol. Chem.
272,
7602
(1997)
[Abstract/Free Full Text]
.
-
J. Sondek,
A. Bohm,
D. G. Lambright,
H. E. Hamm,
P. B. Sigler,
Nature
379,
369
(1996)
[CrossRef] [Medline]
.
-
Recombinant baculovirus containing
bovine H6G2 cDNA was provided by A. Gilman (University
of Texas Southwestern Medical Center, Dallas, TX). The
H6-Q227L-Gs was from T. Patel (University of Tennessee,
Memphis). The baculovirus vector encoding human PLC-2 modified with
an NH2-terminal H6 tag was provided by A. Smrcka (University of Rochester, NY). We thank K. Schey (Medical University of South Carolina, Charleston) for
performing the mass spectrometry analysis on the recombinant
G proteins.
-
Supported as follows: Ford Foundation Fellowship
(C.E.F.), American Heart Association Grant-In-Aid
(N.P.S.), Aaron Diamond Fellowship (G.W.), and both
the Mella and Leon Benziyo Center for Neuroscience and Behavioral
Research and the Joseph Cohn Center for Biomembrane Research (E.R.).
USPHS grants DA02575, DA02121, MH40165, NS33502, DK42086, and DK44840
(R.J.M.); DK38761 and GM54508 (R.I.); and EY06062 and
EY10291 (H.E.H.); Howard Hughes Medical Institute
(L.Y.J. and R.J.L.), a National Institutes of Mental
Health grant to the Silvio Conte Center for
Neuroscience at UCSF (L.Y.J.), and both a Distinguished
Investigator Award from the National Association for Research in
Schizophrenia and Depression and an American Heart Association
Grant-in-Aid (H.E.H.).
26 February 1998; accepted 25 March
1998
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| Full Text »
| PDF »
- Role of {beta}-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease.
- G. S. Lynch and J. G. Ryall (2008)
Physiol Rev
88, 729-767
| Abstract »
| Full Text »
| PDF »
- Dynamic Integration of {alpha}-Adrenergic and Cholinergic Signals in the Atria: ROLE OF G PROTEIN-REGULATED INWARDLY RECTIFYING K+ CHANNELS.
- E. N. Nikolov and T. T. Ivanova-Nikolova (2007)
J. Biol. Chem.
282, 28669-28682
| Abstract »
| Full Text »
| PDF »
- Receptor-Mediated Activation of Heterotrimeric G-Proteins: Current Structural Insights.
- C. A. Johnston and D. P. Siderovski (2007)
Mol. Pharmacol.
72, 219-230
| Abstract »
| Full Text »
| PDF »
- Signaling by a Non-dissociated Complex of G Protein {beta}{gamma} and {alpha} Subunits Stimulated by a Receptor-independent Activator of G Protein Signaling, AGS8.
- C. Yuan, M. Sato, S. M. Lanier, and A. V. Smrcka (2007)
J. Biol. Chem.
282, 19938-19947
| Abstract »
| Full Text »
| PDF »
- G Proteins: More Than Transducers of Receptor-Generated Signals?.
- S. Engelhardt and F. Rochais (2007)
Circ. Res.
100, 1109-1111
| Full Text »
| PDF »
- Human T-cell leukemia virus type-1 Tax oncoprotein regulates G-protein signaling.
- J.-C. Twizere, J.-Y. Springael, M. Boxus, A. Burny, F. Dequiedt, J.-F. Dewulf, J. Duchateau, D. Portetelle, P. Urbain, C. V. Lint, et al. (2007)
Blood
109, 1051-1060
| Abstract »
| Full Text »
| PDF »
- Molecular Determinants for G Protein beta{gamma} Modulation of Ionotropic Glycine Receptors.
- G. E. Yevenes, G. Moraga-Cid, L. Guzman, S. Haeger, L. Oliveira, J. Olate, G. Schmalzing, and L. G. Aguayo (2006)
J. Biol. Chem.
281, 39300-39307
| Abstract »
| Full Text »
| PDF »
- G-Proteins Modulate Cumulative Inactivation of N-Type (CaV2.2) Calcium Channels.
- S. McDavid and K. P. M. Currie (2006)
J. Neurosci.
26, 13373-13383
| Abstract »
| Full Text »
| PDF »
- Direct G Protein Modulation of Cav2 Calcium Channels.
- H. W. Tedford and G. W. Zamponi (2006)
Pharmacol. Rev.
58, 837-862
| Abstract »
| Full Text »
| PDF »
- The molecular basis for T-type Ca2+ channel inhibition by G protein beta2{gamma}2 subunits.
- S. D. DePuy, J. Yao, C. Hu, W. McIntire, I. Bidaud, P. Lory, F. Rastinejad, C. Gonzalez, J. C. Garrison, and P. Q. Barrett (2006)
PNAS
103, 14590-14595
| Abstract »
| Full Text »
| PDF »
- Scanning Mutagenesis Reveals a Role for Serine 189 of the Heterotrimeric G-Protein Beta 1 Subunit in the Inhibition of N-Type Calcium Channels.
- H. W. Tedford, A. E. Kisilevsky, J. B. Peloquin, and G. W. Zamponi (2006)
J Neurophysiol
96, 465-470
| Abstract »
| Full Text »
| PDF »
- Phosducin and Phosducin-like Protein Attenuate G-Protein-Coupled Receptor-Mediated Inhibition of Voltage-Gated Calcium Channels in Rat Sympathetic Neurons.
- J. G. Partridge, H. L. Puhl III, and S. R. Ikeda (2006)
Mol. Pharmacol.
70, 90-100
| Abstract »
| Full Text »
| PDF »
- Direct Modulation of Phospholipase D Activity by Gbeta{gamma}.
- A. M. Preininger, L. G. Henage, W. M. Oldham, E. J. Yoon, H. E. Hamm, and H. A. Brown (2006)
Mol. Pharmacol.
70, 311-318
| Abstract »
| Full Text »
| PDF »
- Differential targeting of Gbetagamma-subunit signaling with small molecules..
- T. M. Bonacci, J. L. Mathews, C. Yuan, D. M. Lehmann, S. Malik, D. Wu, J. L. Font, J. M. Bidlack, and A. V. Smrcka (2006)
Science
312, 443-446
| Abstract »
| Full Text »
| PDF »
- Regions in the G Protein {gamma} Subunit Important for Interaction with Receptors and Effectors.
- C.-S. Myung, W. K. Lim, J. M. DeFilippo, H. Yasuda, R. R. Neubig, and J. C. Garrison (2006)
Mol. Pharmacol.
69, 877-887
| Abstract »
| Full Text »
| PDF »
- Gbeta{gamma} Inhibits G{alpha} GTPase-activating Proteins by Inhibition of G{alpha}-GTP Binding during Stimulation by Receptor.
- W. Tang, Y. Tu, S. K. Nayak, J. Woodson, M. Jehl, and E. M. Ross (2006)
J. Biol. Chem.
281, 4746-4753
| Abstract »
| Full Text »
| PDF »
- Identification of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbeta{gamma}.
- M. Sato, M. J. Cismowski, E. Toyota, A. V. Smrcka, P. A. Lucchesi, W. M. Chilian, and S. M. Lanier (2006)
PNAS
103, 797-802
| Abstract »
| Full Text »
| PDF »
- A Docking Site for G Protein {beta}{gamma} Subunits on the Parathyroid Hormone 1 Receptor Supports Signaling through Multiple Pathways.
- M. J. Mahon, T. M. Bonacci, P. Divieti, and A. V. Smrcka (2006)
Mol. Endocrinol.
20, 136-146
| Abstract »
| Full Text »
| PDF »
- The Regulator of G-Protein Signaling Proteins Involved in Sugar and Abscisic Acid Signaling in Arabidopsis Seed Germination.
- Y. Chen, F. Ji, H. Xie, J. Liang, and J. Zhang (2006)
Plant Physiology
140, 302-310
| Abstract »
| Full Text »
| PDF »
- RACK1 Binds to a Signal Transfer Region of G{beta}{gamma} and Inhibits Phospholipase C {beta}2 Activation.
- S. Chen, F. Lin, and H. E. Hamm (2005)
J. Biol. Chem.
280, 33445-33452
| Abstract »
| Full Text »
| PDF »
- Modulation of calcium currents is eliminated after cleavage of a strategic component of the mammalian secretory apparatus.
- E. M Silinsky (2005)
J. Physiol.
566, 681-688
| Abstract »
| Full Text »
| PDF »
- Ric-8 Enhances G Protein {beta}{gamma}-Dependent Signaling in Response to {beta}{gamma}-Binding Peptides in Intact Cells.
- S. Malik, M. Ghosh, T. M. Bonacci, G. G. Tall, and A. V. Smrcka (2005)
Mol. Pharmacol.
68, 129-136
| Abstract »
| Full Text »
| PDF »
- G Protein {beta}2 Subunit-derived Peptides for Inhibition and Induction of G Protein Pathways: EXAMINATION OF VOLTAGE-GATED Ca2+ AND G PROTEIN INWARDLY RECTIFYING K+ CHANNELS.
- X. Li, A. Hummer, J. Han, M. Xie, K. Melnik-Martinez, R. L. Moreno, M. Buck, M. D. Mark, and S. Herlitze (2005)
J. Biol. Chem.
280, 23945-23959
| Abstract »
| Full Text »
| PDF »
- Activator of G protein signaling 3 regulates opiate activation of protein kinase A signaling and relapse of heroin-seeking behavior.
- L. Yao, K. McFarland, P. Fan, Z. Jiang, Y. Inoue, and I. Diamond (2005)
PNAS
102, 8746-8751
| Abstract »
| Full Text »
| PDF »
- Structure of G Protein-Coupled Receptors and G Proteins.
- R. Iyengar (2005)
Sci. STKE
2005, tr10
| Abstract »
| Full Text »
| PDF »
- Regulatory Interactions between the Amino Terminus of G-protein {beta}{gamma} Subunits and the Catalytic Domain of Phospholipase C{beta}2.
- T. M. Bonacci, M. Ghosh, S. Malik, and A. V. Smrcka (2005)
J. Biol. Chem.
280, 10174-10181
| Abstract »
| Full Text »
| PDF »
- Differential Sensitivity of Phosphatidylinositol 3-Kinase p110{gamma} to Isoforms of G Protein {beta}{gamma} Dimers.
- K. R. Kerchner, R. L. Clay, G. McCleery, N. Watson, W. E. McIntire, C.-S. Myung, and J. C. Garrison (2004)
J. Biol. Chem.
279, 44554-44562
| Abstract »
| Full Text »
| PDF »
- Two types of non-selective cation channel opened by muscarinic stimulation with carbachol in bovine ciliary muscle cells.
- Y. Takai, R. Sugawara, H. Ohinata, and A. Takai (2004)
J. Physiol.
559, 899-922
| Abstract »
| Full Text »
| PDF »
- A Single G{beta} Subunit Locus Controls Cross-talk between Protein Kinase C and G Protein Regulation of N-type Calcium Channels.
- C. J. Doering, A. E. Kisilevsky, Z.-P. Feng, M. I. Arnot, J. Peloquin, J. Hamid, W. Barr, A. Nirdosh, B. Simms, R. J. Winkfein, et al. (2004)
J. Biol. Chem.
279, 29709-29717
| Abstract »
| Full Text »
| PDF »
- Coordination of Membrane Excitability through a GIRK1 Signaling Complex in the Atria.
- E. N. Nikolov and T. T. Ivanova-Nikolova (2004)
J. Biol. Chem.
279, 23630-23636
| Abstract »
| Full Text »
| PDF »
- RACK1 Regulates Specific Functions of G{beta}{gamma}.
- S. Chen, E. J. Dell, F. Lin, J. Sai, and H. E. Hamm (2004)
J. Biol. Chem.
279, 17861-17868
| Abstract »
| Full Text »
| PDF »
- From The Cover: Gi protein activation in intact cells involves subunit rearrangement rather than dissociation.
- M. Bunemann, M. Frank, and M. J. Lohse (2003)
PNAS
100, 16077-16082
| Abstract »
| Full Text »
| PDF »
- Critical Determinants of the G Protein {gamma} Subunits in the G{beta}{gamma} Stimulation of G Protein-activated Inwardly Rectifying Potassium (GIRK) Channel Activity.
- L. Peng, T. Mirshahi, H. Zhang, J. P. Hirsch, and D. E. Logothetis (2003)
J. Biol. Chem.
278, 50203-50211
| Abstract »
| Full Text »
| PDF »
- Insights into G Protein Structure, Function, and Regulation.
- T. M. Cabrera-Vera, J. Vanhauwe, T. O. Thomas, M. Medkova, A. Preininger, M. R. Mazzoni, and H. E. Hamm (2003)
Endocr. Rev.
24, 765-781
| Abstract »
| Full Text »
| PDF »
- Organization and Functions of Interacting Domains for Signaling by Protein-Protein Interactions.
- E. Buck and R. Iyengar (2003)
Sci. STKE
2003, re14
| Abstract »
| Full Text »
| PDF »
- Interaction of G Protein {beta} Subunit with Inward Rectifier K+ Channel Kir3.
- Q. Zhao, T. Kawano, H. Nakata, Y. Nakajima, S. Nakajima, and T. Kozasa (2003)
Mol. Pharmacol.
64, 1085-1091
| Abstract »
| Full Text »
| PDF »
- Mapping the G{beta}{gamma}-binding Sites in GIRK1 and GIRK2 Subunits of the G Protein-activated K+ Channel.
- T. Ivanina, I. Rishal, D. Varon, C. Mullner, B. Frohnwieser-Steinecke, W. Schreibmayer, C. W. Dessauer, and N. Dascal (2003)
J. Biol. Chem.
278, 29174-29183
| Abstract »
| Full Text »
| PDF »
- Custom Distinctions in the Interaction of G-protein {beta} Subunits with N-type (CaV2.2) Versus P/Q-type (CaV2.1) Calcium Channels.
- H. L. Agler, J. Evans, H. M. Colecraft, and D. T. Yue (2003)
J. Gen. Physiol.
121, 495-510
| Abstract »
| Full Text »
| PDF »
- Keeping G Proteins at Bay: A Complex Between G Protein-Coupled Receptor Kinase 2 and G{beta}{gamma}.
- D. T. Lodowski, J. A. Pitcher, W. D. Capel, R. J. Lefkowitz, and J. J. G. Tesmer (2003)
Science
300, 1256-1262
| Abstract »
| Full Text »
| PDF »
- Differential Roles of CB1 and CB2 Cannabinoid Receptors in Mast Cells.
- M.-T. Samson, A. Small-Howard, L. M. N. Shimoda, M. Koblan-Huberson, A. J. Stokes, and H. Turner (2003)
J. Immunol.
170, 4953-4962
| Abstract »
| Full Text »
| PDF »
- Agonist unbinding from receptor dictates the nature of deactivation kinetics of G protein-gated K+ channels.
- A. Benians, J. L. Leaney, and A. Tinker (2003)
PNAS
100, 6239-6244
| Abstract »
| Full Text »
| PDF »
- Heterotrimer Formation, Together with Isoprenylation, Is Required for Plasma Membrane Targeting of Gbeta gamma.
- S. Takida and P. B. Wedegaertner (2003)
J. Biol. Chem.
278, 17284-17290
| Abstract »
| Full Text »
| PDF »
- A splice variant of the G protein {beta}3-subunit implicated in disease states does not modulate ion channels.
- V. Ruiz-Velasco and S. R. Ikeda (2003)
Physiol Genomics
13, 85-95
| Abstract »
| Full Text »
| PDF »
- Role of Dynamic Interactions in Effective Signal Transfer for Gbeta Stimulation of Phospholipase C-beta 2.
- E. Buck, P. Schatz, S. Scarlata, and R. Iyengar (2002)
J. Biol. Chem.
277, 49707-49715
| Abstract »
| Full Text »
| PDF »
- The beta gamma Subunit of Heterotrimeric G Proteins Interacts with RACK1 and Two Other WD Repeat Proteins.
- E. J. Dell, J. Connor, S. Chen, E. G. Stebbins, N. P. Skiba, D. Mochly-Rosen, and H. E. Hamm (2002)
J. Biol. Chem.
277, 49888-49895
| Abstract »
| Full Text »
| PDF »
- Regulation of Angiotensin II-induced G Protein Signaling by Phosducin-like Protein.
- J. N. McLaughlin, C. D. Thulin, S. M. Bray, M. M. Martin, T. S. Elton, and B. M. Willardson (2002)
J. Biol. Chem.
277, 34885-34895
| Abstract »
| Full Text »
| PDF »
- Thrombin Receptors Activate Go Proteins in Endothelial Cells to Regulate Intracellular Calcium and Cell Shape Changes.
- J. F. Vanhauwe, T. O. Thomas, R. D. Minshall, C. Tiruppathi, A. Li, A. Gilchrist, E.-j. Yoon, A. B. Malik, and H. E. Hamm (2002)
J. Biol. Chem.
277, 34143-34149
| Abstract »
| Full Text »
| PDF »
- Role of the G Protein gamma Subunit in beta gamma Complex Modulation of Phospholipase Cbeta Function.
- M. Akgoz, I. Azpiazu, V. Kalyanaraman, and N. Gautam (2002)
J. Biol. Chem.
277, 19573-19578
| Abstract »
| Full Text »
| PDF »
- Dancing with Multiple Partners.
- D. G. Woodside (2002)
Sci. STKE
2002, pe14
| Abstract »
| Full Text »
| PDF »
- Gbeta Residues That Do Not Interact with Galpha Underlie Agonist-independent Activity of K+ Channels.
- T. Mirshahi, L. Robillard, H. Zhang, T. E. Hebert, and D. E. Logothetis (2002)
J. Biol. Chem.
277, 7348-7355
| Abstract »
| Full Text »
| PDF »
- Functional expression and FRET analysis of green fluorescent proteins fused to G-protein subunits in rat sympathetic neurons.
- V. Ruiz-Velasco and S. R Ikeda (2001)
J. Physiol.
537, 679-692
| Abstract »
| Full Text »
| PDF »
- {beta}-Adrenergic Signaling in the Heart: Dual Coupling of the {beta}2-Adrenergic Receptor to Gs and Gi Proteins.
- R.-P. Xiao (2001)
Sci. STKE
2001, re15
| Abstract »
| Full Text »
| PDF »
- Ggamma in Dictyostelium: Its Role in Localization of Gbeta gamma to the Membrane Is Required for Chemotaxis in Shallow Gradients.
- N. Zhang, Y. Long, and P. N. Devreotes (2001)
Mol. Biol. Cell
12, 3204-3213
| Abstract »
| Full Text »
| PDF »
- Mutant G protein alpha subunit activated by Gbeta gamma : A model for receptor activation?.
- P. Rondard, T. Iiri, S. Srinivasan, E. Meng, T. Fujita, and H. R. Bourne (2001)
PNAS
| Abstract »
| Full Text »
- G Protein beta gamma Subunit-Mediated Presynaptic Inhibition: Regulation of Exocytotic Fusion Downstream of Ca2+ Entry.
- T. Blackmer, E. C. Larsen, M. Takahashi, T. F. J. Martin, S. Alford, and H. E. Hamm (2001)
Science
292, 293-297
| Abstract »
| Full Text »
- Functional Compartmentalization of Opioid Desensitization in Primary Sensory Neurons.
- G. M. Samoriski and R. A. Gross (2000)
J. Pharmacol. Exp. Ther.
294, 500-509
| Abstract »
| Full Text »
- Role of C-terminal domains of the G protein beta subunit in the activation of effectors.
- C.-S. Myung and J. C. Garrison (2000)
PNAS
97, 9311-9316
| Abstract »
| Full Text »
| PDF »
- Cloned delta -Opioid Receptors in GH3 Cells Inhibit Spontaneous Ca2+ Oscillations and Prolactin Release Through KIR Channel Activation.
- E. T. Piros, R. C. Charles, L. Song, C. J. Evans, and T. G. Hales (2000)
J Neurophysiol
83, 2691-2698
| Abstract »
| Full Text »
| PDF »
- Gbeta 5gamma 2 Is a Highly Selective Activator of Phospholipid-dependent Enzymes.
- U. Maier, A. Babich, N. Macrez, D. Leopoldt, P. Gierschik, D. Illenberger, and B. Nurnberg (2000)
J. Biol. Chem.
275, 13746-13754
| Abstract »
| Full Text »
| PDF »
- Large and diverse numbers of human diseases with HIKE mutations.
- F. D. Ciccarelli, A. Acciarito, and S. Alberti (2000)
Hum. Mol. Genet.
9, 1001-1007
| Abstract »
| Full Text »
| PDF »
- Gbeta regulation of Na/H exchanger-3 activity in rat renal proximal tubules during development.
- X. X. Li, F. E. Albrecht, J. E. Robillard, G. M. Eisner, and P. A. Jose (2000)
Am J Physiol Regulatory Integrative Comp Physiol
278, R931-R936
| Abstract »
| Full Text »
| PDF »
- Mutational Analysis of Gbeta gamma and Phospholipid Interaction with G Protein-coupled Receptor Kinase 2.
- C. V. Carman, L. S. Barak, C. Chen, L.-Y. Liu-Chen, J. J. Onorato, S. P. Kennedy, M. G. Caron, and J. L. Benovic (2000)
J. Biol. Chem.
275, 10443-10452
| Abstract »
| Full Text »
| PDF »
- Multiple G-Protein beta gamma Combinations Produce Voltage-Dependent Inhibition of N-Type Calcium Channels in Rat Superior Cervical Ganglion Neurons.
- V. Ruiz-Velasco and S. R. Ikeda (2000)
J. Neurosci.
20, 2183-2191
| Abstract »
| Full Text »
| PDF »
- A low resolution model for the interaction of G proteins with G protein-coupled receptors.
- L. Oliveira, A.C.M. Paiva, and G. Vriend (1999)
Protein Eng. Des. Sel.
12, 1087-1095
| Abstract »
| Full Text »
| PDF »
- Channelopathies of inwardly rectifying potassium channels.
- M. R. ABRAHAM, A. JAHANGIR, A. E. ALEKSEEV, and A. TERZIC (1999)
FASEB J
13, 1901-1910
| Abstract »
| Full Text »
- Reciprocal Signaling between Heterotrimeric G Proteins and the p21-stimulated Protein Kinase.
- J. Wang, J. A. Frost, M. H. Cobb, and E. M. Ross (1999)
J. Biol. Chem.
274, 31641-31647
| Abstract »
| Full Text »
| PDF »
- Regions on adenylyl cyclase that are necessary for inhibition of activity by beta gamma and Gialpha subunits of heterotrimeric G proteins.
- C. Wittpoth, K. Scholich, Y. Yigzaw, T. M. Stringfield, and T. B. Patel (1999)
PNAS
96, 9551-9556
| Abstract »
| Full Text »
| PDF »
- Effect of Phosducin on Opioid Receptor Function.
- R. Schulz, A. Wehmeyer, K. Schulz, and J. Murphy (1999)
J. Pharmacol. Exp. Ther.
289, 599-606
| Abstract »
| Full Text »
- KSR-1 Binds to G-protein beta gamma Subunits and Inhibits beta gamma -induced Mitogen-activated Protein Kinase Activation.
- B. Bell, H. Xing, K. Yan, N. Gautam, and A. J. Muslin (1999)
J. Biol. Chem.
274, 7982-7986
| Abstract »
| Full Text »
| PDF »
- Gbeta 5 prevents the RGS7-Galpha o interaction through binding to a distinct Ggamma -like domain found in RGS7 and other RGS proteins.
- K. Levay, J. L. Cabrera, D. K. Satpaev, and V. Z. Slepak (1999)
PNAS
96, 2503-2507
| Abstract »
| Full Text »
| PDF »
- Resolution of a Signal Transfer Region from a General Binding Domain in G for Stimulation of Phospholipase C-2.
- E. Buck, J. Li, Y. Chen, G. Weng, S. Scarlata, and R. Iyengar (1999)
Science
283, 1332-1335
| Abstract »
| Full Text »
- Differential Activity of the G Protein beta 5gamma 2 Subunit at Receptors and Effectors.
- M. A. Lindorfer, C.-S. Myung, Y. Savino, H. Yasuda, R. Khazan, and J. C. Garrison (1998)
J. Biol. Chem.
273, 34429-34436
| Abstract »
| Full Text »
| PDF »
- G-Protein beta -Subunit Specificity in the Fast Membrane-Delimited Inhibition of Ca2+ Channels.
- D. E. Garcia, B. Li, R. E. Garcia-Ferreiro, E. O. Hernandez-Ochoa, K. Yan, N. Gautam, W. A. Catterall, K. Mackie, and B. Hille (1998)
J. Neurosci.
18, 9163-9170
| Abstract »
| Full Text »
| PDF »
- Sites Important for PLCbeta 2 Activation by the G Protein beta gamma Subunit Map to the Sides of the beta Propeller Structure.
- M. P. Panchenko, K. Saxena, Y. Li, S. Charnecki, P. M. Sternweis, T. F. Smith, A. G. Gilman, T. Kozasa, and E. J. Neer (1998)
J. Biol. Chem.
273, 28298-28304
| Abstract »
| Full Text »
| PDF »
- Selection of Gbeta Subunits with Point Mutations That Fail to Activate Specific Signaling Pathways In Vivo: Dissecting Cellular Responses Mediated by a Heterotrimeric G Protein in Dictyostelium discoideum.
- T. Jin, M. Amzel, P. N. Devreotes, and L. Wu (1998)
Mol. Biol. Cell
9, 2949-2961
| Abstract »
| Full Text »
- Selective Role of G Protein gamma Subunits in Receptor Interaction.
- Y. Hou, I. Azpiazu, A. Smrcka, and N. Gautam (2000)
J. Biol. Chem.
275, 38961-38964
| Abstract »
| Full Text »
| PDF »
- Selective Coupling of G Protein beta gamma Complexes to Inhibition of Ca2+ Channels.
- M. Diverse-Pierluissi, W. E. McIntire, C.-S. Myung, M. A. Lindorfer, J. C. Garrison, M. F. Goy, and K. Dunlap (2000)
J. Biol. Chem.
275, 28380-28385
| Abstract »
| Full Text »
| PDF »
- Functional Roles of the Two Domains of Phosducin and Phosducin-like Protein.
- J. R. Savage, J. N. McLaughlin, N. P. Skiba, H. E. Hamm, and B. M. Willardson (2000)
J. Biol. Chem.
275, 30399-30407
| Abstract »
| Full Text »
| PDF »
- Characterization of a Phospholipase C beta 2-Binding Site Near the Amino-terminal Coiled-coil of G Protein beta gamma Subunits.
- D. M. Yoshikawa, K. Bresciano, M. Hatwar, and A. V. Smrcka (2001)
J. Biol. Chem.
276, 11246-11251
| Abstract »
| Full Text »
| PDF »
- Dual Regulation of Akt/Protein Kinase B by Heterotrimeric G Protein Subunits.
- R. K. Bommakanti, S. Vinayak, and W. F. Simonds (2000)
J. Biol. Chem.
275, 38870-38876
| Abstract »
| Full Text »
| PDF »
- G Protein beta Subunit Types Differentially Interact with a Muscarinic Receptor but Not Adenylyl Cyclase Type II or Phospholipase C-beta 2/3.
- Y. Hou, V. Chang, A. B. Capper, R. Taussig, and N. Gautam (2001)
J. Biol. Chem.
276, 19982-19988
| Abstract »
| Full Text »
| PDF »
- Insulin and Insulin-like Growth Factor I Receptors Utilize Different G Protein Signaling Components.
- S. Dalle, W. Ricketts, T. Imamura, P. Vollenweider, and J. M. Olefsky (2001)
J. Biol. Chem.
276, 15688-15695
| Abstract »
| Full Text »
| PDF »
- Interaction Sites of the G Protein beta Subunit with Brain G Protein-coupled Inward Rectifier K+ Channel.
- A. M. Albsoul-Younes, P. M. Sternweis, P. Zhao, H. Nakata, S. Nakajima, Y. Nakajima, and T. Kozasa (2001)
J. Biol. Chem.
276, 12712-12717
| Abstract »
| Full Text »
| PDF »
- The G Protein beta Subunit Is a Determinant in the Coupling of Gs to the beta 1-Adrenergic and A2a Adenosine Receptors.
- W. E. McIntire, G. MacCleery, and J. C. Garrison (2001)
J. Biol. Chem.
276, 15801-15809
| Abstract »
| Full Text »
| PDF »
- Parallel Regulation of Mitogen-activated Protein Kinase Kinase 3 (MKK3) and MKK6 in Gq-signaling Cascade.
- J. Yamauchi, G. Tsujimoto, Y. Kaziro, and H. Itoh (2001)
J. Biol. Chem.
276, 23362-23372
| Abstract »
| Full Text »
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- Regulator of G-protein Signaling 3 (RGS3) Inhibits Gbeta 1gamma 2-induced Inositol Phosphate Production, Mitogen-activated Protein Kinase Activation, and Akt Activation.
- C.-S. Shi, S. B. Lee, S. Sinnarajah, C. W. Dessauer, S. G. Rhee, and J. H. Kehrl (2001)
J. Biol. Chem.
276, 24293-24300
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- Modulation of the G Protein Regulator Phosducin by Ca2+/Calmodulin-dependent Protein Kinase II Phosphorylation and 14-3-3 Protein Binding.
- C. D. Thulin, J. R. Savage, J. N. McLaughlin, S. M. Truscott, W. M. Old, N. G. Ahn, K. A. Resing, H. E. Hamm, M. W. Bitensky, and B. M. Willardson (2001)
J. Biol. Chem.
276, 23805-23815
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- The Role of Electrostatic Interactions in the Regulation of the Membrane Association of G Protein beta gamma Heterodimers.
- D. Murray, S. McLaughlin, and B. Honig (2001)
J. Biol. Chem.
276, 45153-45159
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- RGS12 and RGS14 GoLoco Motifs Are Galpha i Interaction Sites with Guanine Nucleotide Dissociation Inhibitor Activity.
- R. J. Kimple, L. De Vries, H. Tronchere, C. I. Behe, R. A. Morris, M. G. Farquhar, and D. P. Siderovski (2001)
J. Biol. Chem.
276, 29275-29281
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- Modular Design of Gbeta as the Basis for Reversible Specificity in Effector Stimulation.
- E. Buck and R. Iyengar (2001)
J. Biol. Chem.
276, 36014-36019
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- Binding of Galpha o N Terminus Is Responsible for the Voltage-resistant Inhibition of alpha 1A (P/Q-type, Cav2.1) Ca2+ Channels.
- M. Kinoshita, T. Nukada, T. Asano, Y. Mori, A. Akaike, M. Satoh, and S. Kaneko (2001)
J. Biol. Chem.
276, 28731-28738
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- Mutant G protein alpha subunit activated by Gbeta gamma : A model for receptor activation?.
- P. Rondard, T. Iiri, S. Srinivasan, E. Meng, T. Fujita, and H. R. Bourne (2001)
PNAS
98, 6150-6155
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- Cloning, tissue distribution, and functional expression of the human G protein {beta}4-subunit.
- V. RUIZ-VELASCO, S. R. IKEDA, and H. L. PUHL (2002)
Physiol Genomics
8, 41-50
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