PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10727532-4 2000 However a kinase-dead GRK2 mutant (GRK2-K220R) only decreased inositol phosphate production, indicating that GRK2 could regulate Galphaq signaling through a phosphorylation-independent mechanism. Inositol Phosphates 62-80 G protein-coupled receptor kinase 2 Homo sapiens 22-26 15542600-4 2005 Overexpression of GRK2 promoted H1HR phosphorylation in intact HEK293 cells and completely inhibited inositol phosphate production stimulated by H1HR, whereas GRK5 and GRK6 had lesser effects on H1HR phosphorylation and signaling. Inositol Phosphates 101-119 G protein-coupled receptor kinase 2 Homo sapiens 18-22 15542600-5 2005 Interestingly, catalytically inactive GRK2 (GRK2-K220R) also significantly attenuated H1HR-mediated inositol phosphate production, as did an N-terminal fragment of GRK2 previously characterized as a regulator of G protein signaling (RGS) protein for Galpha(q/11). Inositol Phosphates 100-118 G protein-coupled receptor kinase 2 Homo sapiens 38-42 15542600-5 2005 Interestingly, catalytically inactive GRK2 (GRK2-K220R) also significantly attenuated H1HR-mediated inositol phosphate production, as did an N-terminal fragment of GRK2 previously characterized as a regulator of G protein signaling (RGS) protein for Galpha(q/11). Inositol Phosphates 100-118 G protein-coupled receptor kinase 2 Homo sapiens 44-49 15542600-5 2005 Interestingly, catalytically inactive GRK2 (GRK2-K220R) also significantly attenuated H1HR-mediated inositol phosphate production, as did an N-terminal fragment of GRK2 previously characterized as a regulator of G protein signaling (RGS) protein for Galpha(q/11). Inositol Phosphates 100-118 G protein-coupled receptor kinase 2 Homo sapiens 44-48 15542600-6 2005 Disruption of this RGS function in holo-GRK2 by mutation (GRK2-D110A) partially reversed the quenching effect of GRK2, whereas deletion of both the kinase activity and RGS function (GRK2-D110A/K220R) effectively relieved the inhibition of inositol phosphate generation. Inositol Phosphates 239-257 G protein-coupled receptor kinase 2 Homo sapiens 40-44 15542600-6 2005 Disruption of this RGS function in holo-GRK2 by mutation (GRK2-D110A) partially reversed the quenching effect of GRK2, whereas deletion of both the kinase activity and RGS function (GRK2-D110A/K220R) effectively relieved the inhibition of inositol phosphate generation. Inositol Phosphates 239-257 G protein-coupled receptor kinase 2 Homo sapiens 58-62 15542600-6 2005 Disruption of this RGS function in holo-GRK2 by mutation (GRK2-D110A) partially reversed the quenching effect of GRK2, whereas deletion of both the kinase activity and RGS function (GRK2-D110A/K220R) effectively relieved the inhibition of inositol phosphate generation. Inositol Phosphates 239-257 G protein-coupled receptor kinase 2 Homo sapiens 58-62 15542600-6 2005 Disruption of this RGS function in holo-GRK2 by mutation (GRK2-D110A) partially reversed the quenching effect of GRK2, whereas deletion of both the kinase activity and RGS function (GRK2-D110A/K220R) effectively relieved the inhibition of inositol phosphate generation. Inositol Phosphates 239-257 G protein-coupled receptor kinase 2 Homo sapiens 58-62 12486133-6 2003 And indeed, the amino terminus of GRK2 (GRK2(1-185)) inhibited a Gbetagamma-stimulated inositol phosphate signal in cells, purified GRK2(1-185) suppressed the Gbetagamma-stimulated phosphorylation of rhodopsin, and GRK2(1-185) bound directly to purified Gbetagamma subunits. Inositol Phosphates 87-105 G protein-coupled receptor kinase 2 Homo sapiens 34-38 12486133-6 2003 And indeed, the amino terminus of GRK2 (GRK2(1-185)) inhibited a Gbetagamma-stimulated inositol phosphate signal in cells, purified GRK2(1-185) suppressed the Gbetagamma-stimulated phosphorylation of rhodopsin, and GRK2(1-185) bound directly to purified Gbetagamma subunits. Inositol Phosphates 87-105 G protein-coupled receptor kinase 2 Homo sapiens 40-44 12486133-6 2003 And indeed, the amino terminus of GRK2 (GRK2(1-185)) inhibited a Gbetagamma-stimulated inositol phosphate signal in cells, purified GRK2(1-185) suppressed the Gbetagamma-stimulated phosphorylation of rhodopsin, and GRK2(1-185) bound directly to purified Gbetagamma subunits. Inositol Phosphates 87-105 G protein-coupled receptor kinase 2 Homo sapiens 40-44 12486133-6 2003 And indeed, the amino terminus of GRK2 (GRK2(1-185)) inhibited a Gbetagamma-stimulated inositol phosphate signal in cells, purified GRK2(1-185) suppressed the Gbetagamma-stimulated phosphorylation of rhodopsin, and GRK2(1-185) bound directly to purified Gbetagamma subunits. Inositol Phosphates 87-105 G protein-coupled receptor kinase 2 Homo sapiens 40-44 12101219-5 2002 However, mGluR1a-866Delta- and mGluR1b-stimulated inositol phosphate formation is attenuated following GRK2 expression. Inositol Phosphates 50-68 G protein-coupled receptor kinase 2 Homo sapiens 103-107 12101219-6 2002 The expression of the GRK2 C-terminal domain to block membrane translocation of endogenous GRK2 increases mGluR1a-866Delta- and mGluR1b-stimulated inositol phosphate formation, presumably by blocking membrane translocation of GRK2. Inositol Phosphates 147-165 G protein-coupled receptor kinase 2 Homo sapiens 22-26 12101219-6 2002 The expression of the GRK2 C-terminal domain to block membrane translocation of endogenous GRK2 increases mGluR1a-866Delta- and mGluR1b-stimulated inositol phosphate formation, presumably by blocking membrane translocation of GRK2. Inositol Phosphates 147-165 G protein-coupled receptor kinase 2 Homo sapiens 91-95 12101219-6 2002 The expression of the GRK2 C-terminal domain to block membrane translocation of endogenous GRK2 increases mGluR1a-866Delta- and mGluR1b-stimulated inositol phosphate formation, presumably by blocking membrane translocation of GRK2. Inositol Phosphates 147-165 G protein-coupled receptor kinase 2 Homo sapiens 91-95 12101219-7 2002 In contrast, expression of the kinase-deficient GRK2-K220R mutant inhibits inositol phosphate formation by these unphosphorylated receptors. Inositol Phosphates 75-93 G protein-coupled receptor kinase 2 Homo sapiens 48-52 10727532-4 2000 However a kinase-dead GRK2 mutant (GRK2-K220R) only decreased inositol phosphate production, indicating that GRK2 could regulate Galphaq signaling through a phosphorylation-independent mechanism. Inositol Phosphates 62-80 G protein-coupled receptor kinase 2 Homo sapiens 35-39 10727532-4 2000 However a kinase-dead GRK2 mutant (GRK2-K220R) only decreased inositol phosphate production, indicating that GRK2 could regulate Galphaq signaling through a phosphorylation-independent mechanism. Inositol Phosphates 62-80 G protein-coupled receptor kinase 2 Homo sapiens 35-39 8798423-10 1996 Among lipids tested, lipid inositol phosphates, PIP2 and phosphatidylinositol 4-monophosphate, were found to be the most potent activators of GRK2 and were the only lipids that regulated GRK2 in a complex biphasic manner. Inositol Phosphates 27-46 G protein-coupled receptor kinase 2 Homo sapiens 142-146 9353340-7 1997 Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response. Inositol Phosphates 193-211 G protein-coupled receptor kinase 2 Homo sapiens 74-78 8798423-10 1996 Among lipids tested, lipid inositol phosphates, PIP2 and phosphatidylinositol 4-monophosphate, were found to be the most potent activators of GRK2 and were the only lipids that regulated GRK2 in a complex biphasic manner. Inositol Phosphates 27-46 G protein-coupled receptor kinase 2 Homo sapiens 187-191 19564331-5 2009 Here we show that a 2-fold overexpression of GRK2 leads to the attenuation of endogenous mGluR5-mediated inositol phosphate (InsP) formation in striatal neurons and siRNA knockdown of GRK2 expression leads to enhanced mGluR5-mediated InsP formation. Inositol Phosphates 105-123 G protein-coupled receptor kinase 2 Homo sapiens 45-49 19564331-5 2009 Here we show that a 2-fold overexpression of GRK2 leads to the attenuation of endogenous mGluR5-mediated inositol phosphate (InsP) formation in striatal neurons and siRNA knockdown of GRK2 expression leads to enhanced mGluR5-mediated InsP formation. Inositol Phosphates 125-129 G protein-coupled receptor kinase 2 Homo sapiens 45-49 19564331-5 2009 Here we show that a 2-fold overexpression of GRK2 leads to the attenuation of endogenous mGluR5-mediated inositol phosphate (InsP) formation in striatal neurons and siRNA knockdown of GRK2 expression leads to enhanced mGluR5-mediated InsP formation. Inositol Phosphates 234-238 G protein-coupled receptor kinase 2 Homo sapiens 45-49 19564331-5 2009 Here we show that a 2-fold overexpression of GRK2 leads to the attenuation of endogenous mGluR5-mediated inositol phosphate (InsP) formation in striatal neurons and siRNA knockdown of GRK2 expression leads to enhanced mGluR5-mediated InsP formation. Inositol Phosphates 234-238 G protein-coupled receptor kinase 2 Homo sapiens 184-188 17255208-6 2007 Overexpression of GRK 2 or 3 reduced Ca(2+)(e)-dependent inositol phosphate accumulation by more than 70%, whereas a GRK 2 mutant deficient in G alpha(q) binding (D110A) was without major effect. Inositol Phosphates 57-75 G protein-coupled receptor kinase 2 Homo sapiens 18-23