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(Received for publication, August 28, 1996)
From the Department of Pharmacology, The University of Texas
Southwestern Medical Center, Dallas, Texas 75235
ABSTRACT RGS proteins constitute a newly appreciated group
of negative INTRODUCTION Heterotrimeric G protein1 A family of negative regulators of G protein signaling, so-called RGS
proteins, was identified recently as a result of genetic studies in
yeast, worms, and other organisms (8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19). We demonstrated that two of
these proteins, RGS4 and GAIP, act as GAPs on several members of the
Gi subfamily of EXPERIMENTAL PROCEDURES Gs RGS4 (hexahistidine-tagged at the amino terminus) was synthesized
in Escherichia coli as described previously (20), except
that cells were incubated for 12 h at 30 °C after induction.
The bacterial lysate was purified on Ni-NTA resin (Qiagen) as
described, except that 500 mM NaCl was included in the
first wash. Ammonium sulfate (1.2 M final concentration)
was added to the Ni-NTA column eluate, and this solution was applied to
a 15-ml Phenyl-Sepharose FPLC column equilibrated with 50 mM Tris-HCl (pH 8), 2 mM dithiothreitol, and
1.2 M (NH4)2SO4. The
column was washed with 100 ml of equilibration buffer and eluted with a
100-ml continuous gradient of 50 mM Tris-HCl and 1.2 to
0.84 M (NH4)2SO4.
Fractions were analyzed electrophoretically, and protein was pooled and
dialyzed into 50 mM NaHepes (pH 8), 1 mM EDTA,
and 2 mM dithiothreitol prior to concentration and storage.
The yield was 4 mg/liter of bacterial culture. Purified RGS4 was
homogeneous based on sodium dodecyl sulfate-polyacrylamide gel
electrophoresis (see Fig. 5), had the anticipated amino-terminal amino
acid sequence, and displayed a single mass spectroscopic peak
(Mr = 24,183; predicted, 24,188).
GAP assays were performed using
Go Direct measurement of the kcat for GTP
hydrolysis by G12 RESULTS AND DISCUSSION We reported previously that RGS4 and
GAIP accelerate the rate of the GTPase reaction catalyzed by selected
members of the Gi subfamily of
Variation of the substrate (GTP-Go The
crystal structures of the GDP-AlF4 These considerations have prompted examination of the interactions of
RGS4 with the GDP-, GTP
Competition assays (at 150 nM GTP-Go The competition assay just described was
utilized to examine the interactions of RGS4 with other G protein
We also noted previously the inability of RGS4 (or GAIP) to stimulate
GTP hydrolysis by Gs The
data presented above strongly imply formation of a high affinity
complex between RGS4 and the
GDP-AlF4 We conclude that RGS4 has a relatively low affinity (greater than 1 µM) for its substrates, GTP-Gi FOOTNOTES Acknowledgments We thank Drs. Andre Raw, Carmen Dessauer,
Thomas Wilkie, and Stephen Sprang for helpful suggestions.
REFERENCES
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27209-27212
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS AND DISCUSSION
FOOTNOTES
Acknowledgments
REFERENCES
egulators of 
protein
ignaling. Discovered by genetic screens in yeast, worms,
and other organisms, two mammalian RGS proteins, RGS4 and GAIP, act as
GTPase-activating proteins for members of the Gi family of
G protein 
subunits. We have purified recombinant RGS4 to
homogeneity and demonstrate that it acts catalytically to stimulate GTP
hydrolysis by Gi proteins. Furthermore, RGS4 stabilizes the
transition state for GTP hydrolysis, as evidenced by its high affinity
for the
GDP-AlF4
-bound
forms of Go
and Gi and its relatively low
affinity for the GTP
S- and GDP-bound forms of these proteins.
Consequently, RGS4 is most likely not a downstream effector for
activated G subunits. All members of the Gi
subfamily of proteins tested are substrates for RGS4 (including
Gt and Gz); the protein has lower
affinity for Gq, and it does not stimulate the GTPase
activity of Gs or G12.
subunits
cycle between inactive, GDP-bound and active, GTP-bound states, and the
duration of activation is thus dependent on their intrinsic GTPase
activity. Nucleotide hydrolysis by some G proteins is controlled
extrinsically by activating proteins known as GAPs, and the G protein
GAPs described previously are known effectors of the subunit with
which they interact (1). Thus, phospholipase C-
1 is activated by
Gq and, in turn, increases the
kcat for nucleotide hydrolysis by
Gq by roughly 100-fold (2, 3). Gt
interacts similarly with the subunit of a retinal cyclic GMP
phosphodiesterase (4, 5, 6, 7).
subunits (20). However, the mechanism
of this effect and the possibility of other functional relationships
between these GAPs and their target G proteins remained unclear. We
demonstrate herein that purified recombinant RGS4 acts catalytically to
accelerate the GTPase activity of Gi protein family
members, that RGS4 has high affinity for the transition state complex
of the G protein subunit bound to
GDP-AlF4 (but low affinity for
GTPS- and GDP-), and that the rank order of affinities of RGS4
for transition state complexes of subunits is Gi
family > Gq 
Gs. RGS4 has no
detectable GAP activity toward Gs or
G12.
,
Gi1, and Go were expressed and purified
as described (21), as were Gz and G12
(22); Gi1 and Go were myristoylated
unless stated otherwise. Bovine retinal Gt was the
generous gift of Dr. Heidi Hamm (University of Illinois College of
Medicine), while recombinant Gq was supplied by Dr. John
Hepler (this laboratory) (23). Go was activated with 100 µM GTPS and 10 mM MgSO4 by
incubation at 30 °C for 60 min. The indicated GDP-bound subunits
were activated with AlF4 by incubation
with 20 µM AlCl3, 10 mM NaF, and
10 mM MgSO4 for 10 min on ice.
Fig. 5.
RGS4 and
GDP-AlF4-Gi1 form a
high-affinity complex. A, RGS4 (2.2 mg) or
Gi1 (2.2 mg; activated with 20 µM
AlCl3, 10 mM NaF, and 5 mM
MgSO4 for 10 min at 4 °C) was applied to a 16/60
Superdex gel filtration column equilibrated and eluted with 50 mM NaHepes (pH 8), 1 mM EDTA, 10 mM
NaF, 20 µM AlCl3, 5 mM
MgSO4, 2 mM dithiothreitol, and 50 mM NaCl. Fractions (1.5 ml) were collected, and
A280 was monitored. Arrows indicate
the position of molecular weight standards. B, as in
A, except that RGS4 and
GDP-AlF4-Gi1 were
incubated together prior to gel filtration. Fractions were analyzed
electrophoretically, and gels were stained with Coomassie Brilliant
Blue. The higher molecular weight band is Gi1; the lower
is RGS4. C, as in B, except the
Gln204 
Leu mutant of Gi1 was substituted
for the wild type protein.
[View Larger Version of this Image (60K GIF file)]
as the substrate as described previously (20). This
assay relies on formation of a complex between Go and
[-32P]GTP in the absence of Mg2+ and
subsequent initiation of nucleotide hydrolysis by incubation of this
complex at 4 °C with Mg2+ and RGS4. A single round of
hydrolysis of GTP to GDP is then monitored over 5 min by quantification
of release of 32Pi.
and Gz required an
alternative protocol because of their slow rates of nucleotide
exchange. G12 and Gz were incubated with
5 µM [-32P]GTP (20-50 cpm/fmol) and 5 mM EDTA at 30 °C for 30 min. Samples were then
gel-filtered at 4 °C through a Sephadex G-50 spin column (Pharmacia)
equilibrated with 50 mM NaHepes (pH 8), 1 mM
dithiothreitol, 5 mM EDTA, and 0.1%
C12E10 to remove free GTP and Pi.
GTPase activity was measured at 15 °C in 50 µl of the same
solution with addition of 8 mM MgSO4, 1 mM GTP (unlabeled), and the indicated concentration of
RGS4.
subunits by at least
40-fold; the concentrations of RGS proteins utilized in that study were
in excess of those of the G protein substrates. Other
GAPs have been shown to act catalytically (4, 24, 25, 26), and the same is
true of RGS4. Thus, concentrations of RGS4 as low as 2.9 nM
were sufficient to enhance the GTPase activity of 70 nM
GTP-Go (Fig. 1A), and the
initial slopes of the curves in Fig. 1A (from 0 to 29 nM RGS4) are directly proportional to the RGS4
concentration. Thus, in this experiment, 1 mol of RGS4 catalyzed the
turnover of 6 mol of GTP-Go/min at a substrate
(GTP-Go) concentration that is probably more than
20-fold below the Km of GTP-Go for
RGS4. It would be necessary to saturate the substrate with RGS4 to
estimate the maximal enhancement of the rate of GTP hydrolysis; the
rate of hydrolysis of GTP is then too fast to measure with the methods
used herein to monitor release of 32Pi. The
maximal enhancement of the rate of GTP hydrolysis observed in this
experiment was greater than 40-fold.
Fig. 1.
RGS4 acts catalytically to stimulate the
GTPase activity of Go. A, Go
(200 nM; 10 pmol/sample) was incubated with 1 µM [-32P]GTP for 20 min at 20 °C and
then transferred to an ice bath for 5 min. The indicated concentrations
of RGS4 (plus Mg2+) were added at zero time, and release of
32Pi was determined over the indicated time
course at 4 °C. (The estimated concentration of
GTP-Go was 70 nM.) Inset, the
initial rates of Pi release are plotted against the amount
of RGS4. B, varying concentrations of GTP-Go
were incubated with 2.1 nM RGS4 and 15 mM
MgSO4 at 4 °C, and the linear release of
32Pi was monitored over 1 min (7 time points).
These initial rates are plotted against the concentration of
GTP-Go (determined by the maximal amount of
Pi released). Inset, Lineweaver-Burk analysis of
these data. These data represent one of two similar experiments.
[View Larger Version of this Image (18K GIF file)]
) concentration
permitted estimation of the Km for the interaction
of GTP-Go with RGS4 and the maximal rate of turnover of
GTP-Go by RGS4 (Fig. 1B). These values are
2.5 µM and 14/s, respectively, but should be considered
estimates, since the substrate concentration was varied over a
relatively limited range. This turnover rate could be limited by the
maximal intrinsic rate of GTP hydrolysis by Go.
complexes of Gi1 (27) and Gt (28)
revealed that AlF4 occupies the
position normally taken by the -phosphate of GTP but, remarkably,
that the fluorine atoms assume a square planar configuration about the
central aluminum atom, in contrast to the tetrahedral geometry of a
phosphate group. The AlF4 complex is
octahedrally coordinated to a -phosphate oxygen and to the putative
hydrolytic water molecule. Furthermore, an Arg residue and a Gln
residue that are known to be critical for catalysis are dramatically
reoriented in the GDP-AlF4 structure
(compared to their positions in the GTPS-bound protein), contacting
the fluorine atoms and the hydrolytic water. These facts (and others)
argue that GDP-AlF4 is not a GTP
analog but rather mimics the trigonal-bipyramidal species that is
presumed to appear at or near the transition state of the
SN2 reaction.
S-, and
GDP-AlF4-bound forms of
Go by testing the capacity of these proteins to compete
with GTP-Go for its GAP. The basic assay is seen in Fig.
2A. Addition of 2 µM
GDP-Go or GTPS-Go to 200 nM [-32P]GTP-Go had little
or no observable effect on nucleotide hydrolysis stimulated by 29 nM RGS4. However, 2 µM
GDP-AlF4-Go completely
blocked the effect of RGS4, presumably by formation of a high affinity
complex with the GAP. Free guanine nucleotide or the combination of
AlCl3, NaF, and MgSO4 had no effect on
nucleotide hydrolysis in these assays.
Fig. 2.
Inhibition of the effect of RGS4 by
GDP-AlF4-Go.
Go was incubated with 100 µM GTPS at
30 °C for 1 h or with 20 µM AlCl3, 10 mM NaF, and 5 mM MgSO4 for 15 min
on ice. A, the substrate for RGS4 was 200 nM
[-32P]GTP-Go. RGS4 (29 nM)
was incubated on ice with 2 µM GTPS-Go
(
), 2 µM
GDP-AlF4-Go (
), 2 µM GDP-Go (
), or buffer (
) prior to
incubation with [-32P]GTP-Go. One
reaction mixture did not contain RGS4 protein (
). Release of
32Pi was determined as described under
``Experimental Procedures.'' The data shown are representative of
three such experiments. B, the substrate was 140 nM [-32P]GTP-Go. RGS4 (29 nM) was incubated with the indicated concentrations of
GTPS-Go () or
GDP-AlF4-Go () prior
to addition of substrate. The time course of GTP hydrolysis was
determined under these conditions, and each point of the graph
represents the rate determined by curve fitting to nine such time
points. The data shown represent one of two similar experiments.
[View Larger Version of this Image (14K GIF file)]
) with
different concentrations of GTPS-Go or
GDP-AlF4-Go highlight
the preferential affinity of RGS4 for the transition state conformation
of the G protein (Fig. 2B). Stimulated GTP hydrolysis is
nearly completely inhibited at concentrations of
GDP-AlF4-Go that
approximate those of RGS4. The apparent Kd of RGS4
for GDP-AlF4-Go is thus
below 100 nM. Again, GTPS-Go is a poor
competitor (Fig. 2B), consistent with the
Km for GTP-Go estimated in Fig.
1B, as were the GTPS-bound forms of Gz,
Gi1, and Gi3 (not shown).
Subfamily Members and with
Gq but Not with Gs or
G12
subunit family members. We demonstrated previously that RGS4 stimulates
GTP hydrolysis by Gi1, Gi2,
Gi3, and Go. Gi1 and
Go were similarly effective in the competition assay as
the GDP-AlF4-bound species (Fig.
3). Two additional Gi subfamily members were
also tested for interactions with RGS4.
GDP-AlF4-Gt was an
effective competitor (Fig. 3), indistinguishable from
Gi1 and Go. The
kcat for GTP hydrolysis by Gz was
measured directly and was increased from its normal low value of
0.02/min to 0.12/min by 12 nM RGS4 (Fig.
4A). It thus seems likely that the GTPase
activity of all Gi subfamily members is stimulated by RGS4.
We have attempted direct estimation of affinities between
GDP-AlF4-bound subunits and RGS4
by observation of surface plasmon resonance (Pharmacia Biosensor).
Appropriate protein-protein interactions were detected, but the rate of
dissociation of hexahistidine-tagged RGS4 from the Ni-NTA-derivatized
chips of the Biosensor instrument was faster than the rate of
dissociation of
GDP-AlF4-Go from RGS4.
Thus, we can only estimate an upper limit for the Kd
from these experiments, roughly 100 nM.
Fig. 3.
Specificity of the inhibition of RGS4 by
various GDP-4-G
protein complexes. The substrate was 140 nM
[-32P]GTP-Go. RGS4 (29 nM)
was incubated with GDP-AlF4 complexes
of Go (
), Gi1 (), Gt
(), Gq (), or Gs () for 5 min on
ice prior to incubation with the substrate. The time course of GTP
hydrolysis was determined under the indicated conditions, and each
point of the graph represents the rate determined by curve fitting to
nine such time points. The RGS4-stimulated control rate of GTP
hydrolysis ranged from 3.5/min to 6.5/min in various experiments. The
data shown represent one of two similar experiments with each
competitor protein.
[View Larger Version of this Image (23K GIF file)]
Fig. 4.
RGS4 stimulates the GTPase activity of
Gz but not G12.
[-32P]GTP Gz and G12
substrates were prepared as described under ``Experimental
Procedures.'' A,
[-32P]GTP-Gz (2.4 nM) was
incubated with () or without () 12 nM RGS4, and the
rate of GTP hydrolysis was measured at 15 °C. B,
[-32P]GTP-G12 (3 nM) was
incubated with () or without () 0.6 µM RGS4, and
the initial rate of GTP hydrolysis was measured at 15 °C. In both
panels, data shown are averages of duplicate determinations from a
single experiment, which is representative of three such
experiments.
[View Larger Version of this Image (13K GIF file)]
; accordingly, the
GDP-AlF4-bound form of
Gs did not compete with Go (Fig. 3). Of
interest, GDP-AlF4-Gq
did interact with RGS4, although its apparent affinity for the protein
is 10- to 100-fold or more lower than are those of the Gi
subfamily members. However, the assumption that
GDP-AlF4-bound complexes of all G
protein subunits are transition-state mimics may be unwarranted.
Gq must be reconstituted with an appropriate receptor to
examine the effect of RGS4 on nucleotide hydrolysis; the rate of
nucleotide exchange is too low to permit preparation of
GTP-Gq substrate by the present methods. A high
concentration of RGS4 did not stimulate GTP hydrolysis by
G12, which proceeded with a kcat
of 0.06/min at 15 °C (Fig. 4B).
-Gi1
-bound forms of various
Gi proteins. To demonstrate this directly and to prepare
material for crystallographic analysis, we have performed gel
filtration chromatography on mixtures of RGS4 and nonmyristoylated
Gi1; the latter protein has been crystallized previously
in various conformations. Gel-filtered separately, Gi1
and RGS4 elute from a Superdex 200 column at positions consistent with
their monomeric molecular weights (Fig. 5A).
After incubation of
GDP-AlF4-Gi1 with a
modest molar excess of RGS4 on ice for 10 min, the gel filtration
profile reveals formation of a complex of the two proteins, migrating
with an apparent molecular weight of 70,000; free, excess RGS4 is also
seen in its monomeric position (Fig. 5B). The GTPase
activity of the Gln204 Leu mutant of Gi1
is impaired severely. This protein does not interact with
AlF4, and its GTPase activity is not
affected by RGS4 (20, 27). Consistent with these observations, this
protein does not form a high affinity complex with RGS4 when incubated
with AlCl3, NaF, and MgSO4 (Fig.
5C); the elution profiles of the two proteins correspond to
those observed in Fig. 5A.
family
members, but interacts directly and with high affinity with the
transition-state conformations of these subunits. Stabilization of
the transition state lowers the activation energy barrier for
hydrolysis of GTP, accounting for the large rate enhancements that are
seen. We surmise that RGS4 is not an effector for Gi
proteins, based on the relatively poor affinity of RGS4 for their
GTPS-bound forms compared to those of other known effectors of G
protein subunits. We note, however, that some other RGS proteins
are considerably larger than are RGS4 or GAIP, and generalization of
this point may be unwarranted. Finally, we call attention to the recent
observation by Mittal et al. (29) that wild-type
p21ras protein interacts with
AlF4 only in the presence of its GAPs.
Thus, the ground state of p21ras must be too distant,
conformationally, from the transition state to recognize
AlF4 (unlike heterotrimeric G
proteins), but GAPs for low molecular weight GTPases and RGS proteins
both appear to act predominantly by stabilizing the transition states
for nucleotide hydrolysis and not by elevating the energy level of the
enzyme-substrate complex.
Member of the Cell Regulation Graduate Program of University of
Texas Southwestern Graduate School of Biomedical Sciences. Supported by
the Medical Scientist Training Program and Pharmacological Sciences
Training Grant GM07062.
§
To whom correspondence should be addressed: Dept. of Pharmacology,
The University of Texas Southwestern Medical Center, 5323 Harry Hines
Blvd., Dallas, TX 75235.
1
The abbreviations used are: G proteins,
heterotrimeric guanine nucleotide-binding proteins; GAP,
GTPase-activating protein; GTPS, guanosine
5
-(3-O-thio)triphosphate; C12E10,
polyoxyethylene-10-lauryl ether.
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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Y. Yamaguchi, H. Katoh, and M. Negishi N-terminal Short Sequences of alpha Subunits of the G12 Family Determine Selective Coupling to Receptors J. Biol. Chem., April 18, 2003; 278(17): 14936 - 14939. [Abstract] [Full Text] [PDF]
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Z. Chen, W. D. Singer, C. D. Wells, S. R. Sprang, and P. C. Sternweis Mapping the Galpha 13 Binding Interface of the rgRGS Domain of p115RhoGEF J. Biol. Chem., March 7, 2003; 278(11): 9912 - 9919. [Abstract] [Full Text] [PDF]
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 M. J. Kennedy, M. E. Sowa, T. G. Wensel, and J. B. Hurley Acceleration of Key Reactions as a Strategy to Elucidate the Rate-Limiting Chemistry Underlying Phototransduction Inactivation Invest. Ophthalmol. Vis. Sci., March 1, 2003; 44(3): 1016 - 1022. [Abstract] [Full Text] [PDF]
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Y. Wang, G. Ho, J. J. Zhang, B. Nieuwenhuijsen, W. Edris, P. K. Chanda, and K. H. Young Regulator of G Protein Signaling Z1 (RGSZ1) Interacts with Galpha i Subunits and Regulates Galpha i-mediated Cell Signaling J. Biol. Chem., December 6, 2002; 277(50): 48325 - 48332. [Abstract] [Full Text] [PDF]
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 K. Yamagishi, T. Kimura, M. Suzuki, and H. Shinmoto Suppression of fruit-body formation by constitutively active G-protein {alpha}-subunits ScGP-A and ScGP-C in the homobasidiomycete Schizophyllum commune Microbiology, September 1, 2002; 148(9): 2797 - 2809. [Abstract] [Full Text] [PDF]
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 S. Hollinger and J. R. Hepler Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling Pharmacol. Rev., September 1, 2002; 54(3): 527 - 559. [Abstract] [Full Text] [PDF]
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M. A. Booden, D. P. Siderovski, and C. J. Der Leukemia-Associated Rho Guanine Nucleotide Exchange Factor Promotes G{alpha}q-Coupled Activation of RhoA Mol. Cell. Biol., June 15, 2002; 22(12): 4053 - 4061. [Abstract] [Full Text] [PDF]
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 B.-E Xu, K. R. Skowronek, and J. Kurjan The N Terminus of Saccharomyces cerevisiae Sst2p Plays an RGS-Domain-Independent, Mpt5p-Dependent Role in Recovery From Pheromone Arrest Genetics, December 1, 2001; 159(4): 1559 - 1571. [Abstract] [Full Text] [PDF]
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 B. Zheng, Y.-C. Ma, R. S. Ostrom, C. Lavoie, G. N. Gill, P. A. Insel, X.-Y. Huang, and M. G. Farquhar RGS-PX1, a GAP for Galpha s and Sorting Nexin in Vesicular Trafficking Science, November 30, 2001; 294(5548): 1939 - 1942. [Abstract] [Full Text] [PDF]
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R. Vaiskunaite, T. Kozasa, and T. A. Voyno-Yasenetskaya Interaction between the Galpha Subunit of Heterotrimeric G12 Protein and Hsp90 Is Required for Galpha 12 Signaling J. Biol. Chem., November 30, 2001; 276(49): 46088 - 46093. [Abstract] [Full Text] [PDF]
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 K. M. Druey Bridging with GAPs: Receptor Communication Through RGS Proteins Sci. Signal., October 16, 2001; 2001(104): re14 - re14. [Abstract] [Full Text] [PDF]
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 V.J Owen, P.B.J Burton, A.J Mullen, E.J Birks, P Barton, and M.H Yacoub Expression of RGS3, RGS4 and Gi alpha 2 in acutely failing donor hearts and end-stage heart failure Eur. Heart J., June 2, 2001; 22(12): 1015 - 1020. [Abstract] [PDF]
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H. Zhong and R. R. Neubig Regulator of G Protein Signaling Proteins: Novel Multifunctional Drug Targets J. Pharmacol. Exp. Ther., June 1, 2001; 297(3): 837 - 845. [Abstract] [Full Text]
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L. Wang, R. K. Sunahara, A. Krumins, G. Perkins, M. L. Crochiere, M. Mackey, S. Bell, M. H. Ellisman, and S. S. Taylor Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein PNAS, March 13, 2001; 98(6): 3220 - 3225. [Abstract] [Full Text] [PDF]
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 K. B. Lengeler, R. C. Davidson, C. D'souza, T. Harashima, W.-C. Shen, P. Wang, X. Pan, M. Waugh, and J. Heitman Signal Transduction Cascades Regulating Fungal Development and Virulence Microbiol. Mol. Biol. Rev., December 1, 2000; 64(4): 746 - 785. [Abstract] [Full Text] [PDF]
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T. J. Fowler and M. F. Mitton Scooter, a New Active Transposon in Schizophyllum commune, Has Disrupted Two Genes Regulating Signal Transduction Genetics, December 1, 2000; 156(4): 1585 - 1594. [Abstract] [Full Text]
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A. Scheschonka, C. W. Dessauer, S. Sinnarajah, P. Chidiac, C.-S. Shi, and J. H. Kehrl RGS3 Is a GTPase-Activating Protein for Gialpha and Gqalpha and a Potent Inhibitor of Signaling by GTPase-Deficient Forms of Gqalpha and G11alpha Mol. Pharmacol., October 1, 2000; 58(4): 719 - 728. [Abstract] [Full Text]
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 K. S. Murthy, J. R. Grider, and G. M. Makhlouf Heterologous desensitization of response mediated by selective PKC-dependent phosphorylation of Gi-1 and Gi-2 Am J Physiol Cell Physiol, October 1, 2000; 279(4): C925 - C934. [Abstract] [Full Text] [PDF]
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 B. M. Sullivan, K. J. Harrison-Lavoie, V. Marshansky, H. Y. Lin, J. H. Kehrl, D. A. Ausiello, D. Brown, and K. M. Druey RGS4 and RGS2 Bind Coatomer and Inhibit COPI Association with Golgi Membranes and Intracellular Transport Mol. Biol. Cell, September 1, 2000; 11(9): 3155 - 3168. [Abstract] [Full Text]
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S.-W. Jeong and S. R. Ikeda Endogenous Regulator of G-Protein Signaling Proteins Modify N-Type Calcium Channel Modulation in Rat Sympathetic Neurons J. Neurosci., June 15, 2000; 20(12): 4489 - 4496. [Abstract] [Full Text] [PDF]
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M. Sallese, S. Mariggiò, E. D'Urbano, L. Iacovelli, and A. De Blasi Selective Regulation of Gq Signaling by G Protein-Coupled Receptor Kinase 2: Direct Interaction of Kinase N Terminus with Activated Galpha q Mol. Pharmacol., April 1, 2000; 57(4): 826 - 831. [Abstract] [Full Text]
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 Y. Chen and N. J. Penington Competition Between Internal AlF4- and Receptor-Mediated Stimulation of Dorsal Raphe Neuron G-Proteins Coupled to Calcium Current Inhibition J Neurophysiol, March 1, 2000; 83(3): 1273 - 1282. [Abstract] [Full Text] [PDF]
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 C. Moratz, V. H. Kang, K. M. Druey, C.-S. Shi, A. Scheschonka, P. M. Murphy, T. Kozasa, and J. H. Kehrl Regulator of G Protein Signaling 1 (RGS1) Markedly Impairs Gi{alpha} Signaling Responses of B Lymphocytes J. Immunol., February 15, 2000; 164(4): 1829 - 1838. [Abstract] [Full Text] [PDF]
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C. V. Carman, J.-L. Parent, P. W. Day, A. N. Pronin, P. M. Sternweis, P. B. Wedegaertner, A. G. Gilman, J. L. Benovic, and T. Kozasa Selective Regulation of Galpha q/11 by an RGS Domain in the G Protein-coupled Receptor Kinase, GRK2 J. Biol. Chem., November 26, 1999; 274(48): 34483 - 34492. [Abstract] [Full Text] [PDF]
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B. A. Posner, A. G. Gilman, and B. A. Harris Regulators of G Protein Signaling 6 and 7. PURIFICATION OF COMPLEXES WITH Gbeta 5 AND ASSESSMENT OF THEIR EFFECTS ON G PROTEIN-MEDIATED SIGNALING PATHWAYS J. Biol. Chem., October 22, 1999; 274(43): 31087 - 31093. [Abstract] [Full Text] [PDF]
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 Y. M. Hajdu-Cronin, W. J. Chen, G. Patikoglou, M. R. Koelle, and P. W. Sternberg Antagonism between Goalpha and Gqalpha in Caenorhabditis elegans: the RGS protein EAT-16 is necessary for Goalpha signaling and regulates Gqalpha activity Genes & Dev., July 15, 1999; 13(14): 1780 - 1793. [Abstract] [Full Text]
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K. M. Druey, O. Ugur, J. M. Caron, C.-K. Chen, P. S. Backlund, and T. L. Z. Jones Amino-terminal Cysteine Residues of RGS16 Are Required for Palmitoylation and Modulation of Gi- and Gq-mediated Signaling J. Biol. Chem., June 25, 1999; 274(26): 18836 - 18842. [Abstract] [Full Text] [PDF]
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D. S. Woulfe and J. M. Stadel Structural Basis for the Selectivity of the RGS Protein, GAIP, for Galpha i Family Members. IDENTIFICATION OF A SINGLE AMINO ACID DETERMINANT FOR SELECTIVE INTERACTION OF Galpha i SUBUNITS WITH GAIP J. Biol. Chem., June 18, 1999; 274(25): 17718 - 17724. [Abstract] [Full Text] [PDF]
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E. Kim, T. Arnould, L. Sellin, T. Benzing, N. Comella, O. Kocher, L. Tsiokas, V. P. Sukhatme, and G. Walz Interaction between RGS7 and polycystin PNAS, May 25, 1999; 96(11): 6371 - 6376. [Abstract] [Full Text] [PDF]
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O. Saitoh, Y. Kubo, M. Odagiri, M. Ichikawa, K. Yamagata, and T. Sekine RGS7 and RGS8 Differentially Accelerate G Protein-mediated Modulation of K+ Currents J. Biol. Chem., April 2, 1999; 274(14): 9899 - 9904. [Abstract] [Full Text] [PDF]
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 W. Gruning, T. Arnould, F. Jochimsen, L. Sellin, S. Ananth, E. Kim, and G. Walz Modulation of renal tubular cell function by RGS3 Am J Physiol Renal Physiol, April 1, 1999; 276(4): F535 - F543. [Abstract] [Full Text] [PDF]
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K. Levay, J. L. Cabrera, D. K. Satpaev, and V. Z. Slepak Gbeta 5 prevents the RGS7-Galpha o interaction through binding to a distinct Ggamma -like domain found in RGS7 and other RGS proteins PNAS, March 2, 1999; 96(5): 2503 - 2507. [Abstract] [Full Text] [PDF]
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X. Xu, W. Zeng, S. Popov, D. M. Berman, I. Davignon, K. Yu, D. Yowe, S. Offermanns, S. Muallem, and T. M. Wilkie RGS Proteins Determine Signaling Specificity of Gq-coupled Receptors J. Biol. Chem., February 5, 1999; 274(6): 3549 - 3556. [Abstract] [Full Text] [PDF]
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F. Wylie, K. Heimann, T. L. Le, D. Brown, G. Rabnott, and J. L. Stow GAIP, a Galpha i-3-binding protein, is associated with Golgi-derived vesicles and protein trafficking Am J Physiol Cell Physiol, February 1, 1999; 276(2): C497 - C506. [Abstract] [Full Text] [PDF]
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Y. Zhang, S. Y. Neo, J. Han, L. P. Yaw, and S.-C. Lin RGS16 Attenuates Galpha q-dependent p38 Mitogen-activated Protein Kinase Activation by Platelet-activating Factor J. Biol. Chem., January 29, 1999; 274(5): 2851 - 2857. [Abstract] [Full Text] [PDF]
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N. O. Dulin, A. Sorokin, E. Reed, S. Elliott, J. H. Kehrl, and M. J. Dunn RGS3 Inhibits G Protein-Mediated Signaling via Translocation to the Membrane and Binding to Galpha 11 Mol. Cell. Biol., January 1, 1999; 19(1): 714 - 723. [Abstract] [Full Text] [PDF]
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W. Zeng, X. Xu, S. Popov, S. Mukhopadhyay, P. Chidiac, J. Swistok, W. Danho, K. A. Yagaloff, S. L. Fisher, E. M. Ross, et al. The N-terminal Domain of RGS4 Confers Receptor-selective Inhibition of G Protein Signaling J. Biol. Chem., December 25, 1998; 273(52): 34687 - 34690. [Abstract] [Full Text] [PDF]
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M. Bunemann and M. M. Hosey Regulators of G Protein Signaling (RGS) Proteins Constitutively Activate Gbeta gamma -gated Potassium Channels J. Biol. Chem., November 20, 1998; 273(47): 31186 - 31190. [Abstract] [Full Text] [PDF]
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B. E. Snow, A. M. Krumins, G. M. Brothers, S.-F. Lee, M. A. Wall, S. Chung, J. Mangion, S. Arya, A. G. Gilman, and D. P. Siderovski A G protein gamma subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gbeta 5 subunits PNAS, October 27, 1998; 95(22): 13307 - 13312. [Abstract] [Full Text] [PDF]
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E. P. Bowman, J. J. Campbell, K. M. Druey, A. Scheschonka, J. H. Kehrl, and E. C. Butcher Regulation of Chemotactic and Proadhesive Responses to Chemoattractant Receptors by RGS (Regulator of G-protein Signaling) Family Members J. Biol. Chem., October 23, 1998; 273(43): 28040 - 28048. [Abstract] [Full Text] [PDF]
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J. Wang, A. Ducret, Y. Tu, T. Kozasa, R. Aebersold, and E. M. Ross RGSZ1, a Gz-selective RGS Protein in Brain. STRUCTURE, MEMBRANE ASSOCIATION, REGULATION BY Galpha z PHOSPHORYLATION, AND RELATIONSHIP TO A Gz GTPase-ACTIVATING PROTEIN SUBFAMILY J. Biol. Chem., October 2, 1998; 273(40): 26014 - 26025. [Abstract] [Full Text] [PDF]
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M. Natochin, A. E. Granovsky, and N. O. Artemyev Identification of Effector Residues on Photoreceptor G Protein, Transducin J. Biol. Chem., August 21, 1998; 273(34): 21808 - 21815. [Abstract] [Full Text] [PDF]
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K. M. Druey, B. M. Sullivan, D. Brown, E. R. Fischer, N. Watson, K. J. Blumer, C. R. Gerfen, A. Scheschonka, and J. H. Kehrl Expression of GTPase-deficient Gialpha 2 Results in Translocation of Cytoplasmic RGS4 to the Plasma Membrane J. Biol. Chem., July 17, 1998; 273(29): 18405 - 18410. [Abstract] [Full Text] [PDF]
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T. Kozasa, X. Jiang, M. J. Hart, P. M. Sternweis, W. D. Singer, A. G. Gilman, G. Bollag, and P. C. Sternweis p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science, June 26, 1998; 280(5372): 2109 - 2111. [Abstract] [Full Text]
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M. J. Hart, X. Jiang, T. Kozasa, W. Roscoe, W. D. Singer, A. G. Gilman, P. C. Sternweis, and G. Bollag Direct Stimulation of the Guanine Nucleotide Exchange Activity of p115 RhoGEF by G  13Science, June 26, 1998; 280(5372): 2112 - 2114. [Abstract] [Full Text]
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K.-L. Lan, N. A. Sarvazyan, R. Taussig, R. G. Mackenzie, P. R. DiBello, H. G. Dohlman, and R. R. Neubig A Point Mutation in Galpha o and Galpha i1 Blocks Interaction with Regulator of G Protein Signaling Proteins J. Biol. Chem., May 22, 1998; 273(21): 12794 - 12797. [Abstract] [Full Text] [PDF]
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 K. L. Dodge and B. M. Sanborn Evidence for Inhibition by Protein Kinase A of Receptor/G{alpha}q/Phospholipase C (PLC) Coupling by a Mechanism Not Involving PLC{beta}2 Endocrinology, May 1, 1998; 139(5): 2265 - 2271. [Abstract] [Full Text] [PDF]
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L. De Vries, E. Elenko, J. M. McCaffery, T. Fischer, L. Hubler, T. McQuistan, N. Watson, and M. G. Farquhar RGS-GAIP, a GTPase-activating Protein for Galpha i Heterotrimeric G Proteins, Is Located on Clathrin-coated Vesicles Mol. Biol. Cell, May 1, 1998; 9(5): 1123 - 1134. [Abstract] [Full Text]
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M. Natochin, R. L. McEntaffer, and N. O. Artemyev Mutational Analysis of the Asn Residue Essential for RGS Protein Binding to G-proteins J. Biol. Chem., March 20, 1998; 273(12): 6731 - 6735. [Abstract] [Full Text] [PDF]
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P. R. DiBello, T. R. Garrison, D. M. Apanovitch, G. Hoffman, D. J. Shuey, K. Mason, M. I. Cockett, and H. G. Dohlman Selective Uncoupling of RGS Action by a Single Point Mutation in the G Protein alpha -Subunit J. Biol. Chem., March 6, 1998; 273(10): 5780 - 5784. [Abstract] [Full Text] [PDF]
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S. Vincent, M. Brouns, M. J. Hart, and J. Settleman Evidence for distinct mechanisms of transition state stabilization of GTPases by fluoride PNAS, March 3, 1998; 95(5): 2210 - 2215. [Abstract] [Full Text] [PDF]
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M. Natochin and N. O. Artemyev Substitution of Transducin Ser202 by Asp Abolishes G-protein/RGS Interaction J. Biol. Chem., February 20, 1998; 273(8): 4300 - 4303. [Abstract] [Full Text] [PDF]
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D. M. Berman and A. G. Gilman Mammalian RGS Proteins: Barbarians at the Gate J. Biol. Chem., January 16, 1998; 273(3): 1269 - 1272. [Full Text] [PDF]
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S. P. Srinivasa, N. Watson, M. C. Overton, and K. J. Blumer Mechanism of RGS4, a GTPase-activating Protein for G Protein alpha Subunits J. Biol. Chem., January 16, 1998; 273(3): 1529 - 1533. [Abstract] [Full Text] [PDF]
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S. P. Heximer, N. Watson, M. E. Linder, K. J. Blumer, and J. R. Hepler RGS2/G0S8 is a selective inhibitor of Gqalpha function PNAS, December 23, 1997; 94(26): 14389 - 14393. [Abstract] [Full Text] [PDF]
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K. M. Druey and J. H. Kehrl Inhibition of regulator of G protein signaling function by two mutant RGS4 proteins PNAS, November 25, 1997; 94(24): 12851 - 12856. [Abstract] [Full Text] [PDF]
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S. J. Gold, Y. G. Ni, H. G. Dohlman, and E. J. Nestler Regulators of G-Protein Signaling (RGS) Proteins: Region-Specific Expression of Nine Subtypes in Rat Brain J. Neurosci., October 15, 1997; 17(20): 8024 - 8037. [Abstract] [Full Text] [PDF]
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K. Scheffzek, M. R. Ahmadian, W. Kabsch, L. Wiesmüller, A. Lautwein, F. Schmitz, and A. Wittinghofer The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants Science, July 18, 1997; 277(5324): 333 - 338. [Abstract] [Full Text]
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M. Natochin, A. E. Granovsky, and N. O. Artemyev Regulation of Transducin GTPase Activity by Human Retinal RGS J. Biol. Chem., July 11, 1997; 272(28): 17444 - 17449. [Abstract] [Full Text] [PDF]
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S. Popov, K. Yu, T. Kozasa, and T. M. Wilkie The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro PNAS, July 8, 1997; 94(14): 7216 - 7220. [Abstract] [Full Text] [PDF]
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T. K. Chatterjee, A. K. Eapen, and R. A. Fisher A Truncated Form of RGS3 Negatively Regulates G Protein-coupled Receptor Stimulation of Adenylyl Cyclase and Phosphoinositide Phospholipase C J. Biol. Chem., June 13, 1997; 272(24): 15481 - 15487. [Abstract] [Full Text] [PDF]
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C. Huang, J. R. Hepler, A. G. Gilman, and S. M. Mumby Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells PNAS, June 10, 1997; 94(12): 6159 - 6163. [Abstract] [Full Text] [PDF]
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Y. Yan, P. P. Chi, and H. R. Bourne RGS4 Inhibits Gq-mediated Activation of Mitogen-activated Protein Kinase and Phosphoinositide Synthesis J. Biol. Chem., May 2, 1997; 272(18): 11924 - 11927. [Abstract] [Full Text] [PDF]
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T. Wieland, C.-K. Chen, and M. I. Simon The Retinal Specific Protein RGS-r Competes with the gamma Subunit of cGMP Phosphodiesterase for the alpha Subunit of Transducin and Facilitates Signal Termination J. Biol. Chem., April 4, 1997; 272(14): 8853 - 8856. [Abstract] [Full Text] [PDF]
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E. Faurobert and J. B. Hurley The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro PNAS, April 1, 1997; 94(7): 2945 - 2950. [Abstract] [Full Text] [PDF]
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C. Chen, B. Zheng, J. Han, and S.-C. Lin Characterization of a Novel Mammalian RGS Protein That Binds to Galpha Proteins and Inhibits Pheromone Signaling in Yeast J. Biol. Chem., March 28, 1997; 272(13): 8679 - 8685. [Abstract] [Full Text] [PDF]
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J. Wang, Y. Tu, J. Woodson, X. Song, and E. M. Ross A GTPase-activating Protein for the G Protein Galpha z. IDENTIFICATION, PURIFICATION, AND MECHANISM OF ACTION J. Biol. Chem., February 28, 1997; 272(9): 5732 - 5740. [Abstract] [Full Text] [PDF]
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J. R. Hepler, D. M. Berman, A. G. Gilman, and T. Kozasa RGS4 and GAIP are GTPase-activating proteins for Gqalpha and block activation of phospholipase Cbeta by gamma -thio-GTP-Gqalpha PNAS, January 21, 1997; 94(2): 428 - 432. [Abstract] [Full Text] [PDF]
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N. P. Skiba, J. A. Hopp, and V. Y. Arshavsky The Effector Enzyme Regulates the Duration of G Protein Signaling in Vertebrate Photoreceptors by Increasing the Affinity between Transducin and RGS Protein J. Biol. Chem., October 13, 2000; 275(42): 32716 - 32720. [Abstract] [Full Text] [PDF]
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E. P. Marin, A. G. Krishna, and T. P. Sakmar Rapid Activation of Transducin by Mutations Distant from the Nucleotide-binding Site. EVIDENCE FOR A MECHANISTIC MODEL OF RECEPTOR-CATALYZED NUCLEOTIDE EXCHANGE BY G PROTEINS J. Biol. Chem., July 13, 2001; 276(29): 27400 - 27405. [Abstract] [Full Text] [PDF]
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T. K. Chatterjee and R. A. Fisher Novel Alternative Splicing and Nuclear Localization of Human RGS12 Gene Products J. Biol. Chem., September 15, 2000; 275(38): 29660 - 29671. [Abstract] [Full Text] [PDF]
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D. S. Witherow, Q. Wang, K. Levay, J. L. Cabrera, J. Chen, G. B. Willars, and V. Z. Slepak Complexes of the G Protein Subunit Gbeta 5 with the Regulators of G Protein Signaling RGS7 and RGS9. CHARACTERIZATION IN NATIVE TISSUES AND IN TRANSFECTED CELLS J. Biol. Chem., August 4, 2000; 275(32): 24872 - 24880. [Abstract] [Full Text] [PDF]
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R. Vaiskunaite, V. Adarichev, H. Furthmayr, T. Kozasa, A. Gudkov, and T. A. Voyno-Yasenetskaya Conformational Activation of Radixin by G13 Protein alpha Subunit J. Biol. Chem., August 18, 2000; 275(34): 26206 - 26212. [Abstract] [Full Text] [PDF]
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T. K. Chatterjee and R. A. Fisher Cytoplasmic, Nuclear, and Golgi Localization of RGS Proteins. EVIDENCE FOR N-TERMINAL AND RGS DOMAIN SEQUENCES AS INTRACELLULAR TARGETING MOTIFS J. Biol. Chem., July 28, 2000; 275(31): 24013 - 24021. [Abstract] [Full Text] [PDF]
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U. Rumenapp, M. Asmus, H. Schablowski, M. Woznicki, L. Han, K. H. Jakobs, M. Fahimi-Vahid, C. Michalek, T. Wieland, and M. Schmidt The M3 Muscarinic Acetylcholine Receptor Expressed in HEK-293 Cells Signals to Phospholipase D via G12 but Not Gq-type G Proteins. REGULATORS OF G PROTEINS AS TOOLS TO DISSECT PERTUSSIS TOXIN-RESISTANT G PROTEINS IN RECEPTOR-EFFECTOR COUPLING J. Biol. Chem., January 19, 2001; 276(4): 2474 - 2479. [Abstract] [Full Text] [PDF]
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G. A. Hoffman, T. R. Garrison, and H. G. Dohlman Endoproteolytic Processing of Sst2, a Multidomain Regulator of G Protein Signaling in Yeast J. Biol. Chem., November 22, 2000; 275(48): 37533 - 37541. [Abstract] [Full Text] [PDF]
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K.-L. Lan, H. Zhong, M. Nanamori, and R. R. Neubig Rapid Kinetics of Regulator of G-protein Signaling (RGS)-mediated Galpha i and Galpha o Deactivation. Galpha SPECIFICITY OF RGS4 AND RGS7 J. Biol. Chem., October 20, 2000; 275(43): 33497 - 33503. [Abstract] [Full Text] [PDF]
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M. L. Cunningham, G. L. Waldo, S. Hollinger, J. R. Hepler, and T. K. Harden Protein Kinase C Phosphorylates RGS2 and Modulates Its Capacity for Negative Regulation of Galpha 11 Signaling J. Biol. Chem., February 16, 2001; 276(8): 5438 - 5444. [Abstract] [Full Text] [PDF]
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P. G. Burgon, W. L. Lee, A. B. Nixon, E. G. Peralta, and P. J. Casey Phosphorylation and Nuclear Translocation of a Regulator of G Protein Signaling (RGS10) J. Biol. Chem., August 24, 2001; 276(35): 32828 - 32834. [Abstract] [Full Text] [PDF]
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