The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro. - Wikidata - awgldk - TriplyDB

The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.

The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.

http://www.wikidata.org/entity/Q36072644

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GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G proteins, is located on clathrin-coated vesicles RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins RGS2/G0S8 is a selective inhibitor of Gqalpha function Clathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitro The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae Promotion of G alpha i3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP RGS7 and RGS8 differentially accelerate G protein-mediated modulation of K+ currents G beta 5.RGS7 inhibits G alpha q-mediated signaling via a direct protein-protein interaction Interaction of human retinal RGS with G-protein alpha-subunits Expression of GTPase-deficient Gialpha2 results in translocation of cytoplasmic RGS4 to the plasma membrane RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells Mechanism of RGS4, a GTPase-activating protein for G protein alpha subunits Regulators of G Protein Signaling Structural Basis for the Selectivity of the RGS Protein, GAIP, for G i Family Members: IDENTIFICATION OF A SINGLE AMINO ACID DETERMINANT FOR SELECTIVE INTERACTION OF G i SUBUNITS WITH GAIP G(z) signaling: emerging divergence from G(i) signaling.Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members.Antagonism between G(o)alpha and G(q)alpha in Caenorhabditis elegans: the RGS protein EAT-16 is necessary for G(o)alpha signaling and regulates G(q)alpha activity Regulators of G protein signaling attenuate the G protein-mediated inhibition of N-type Ca channels Gbeta5-RGS complexes co-localize with mGluR6 in retinal ON-bipolar cells A physiologically required G protein-coupled receptor (GPCR)-regulator of G protein signaling (RGS) interaction that compartmentalizes RGS activity.Timing is everything: GTPase regulation in phototransduction.Regulator of G Protein Signaling 17 as a Negative Modulator of GPCR Signaling in Multiple Human Cancers.Endoproteolytic processing of Sst2, a multidomain regulator of G protein signaling in yeast.RGS Protein Regulation of Phototransduction.Regulators of G protein signaling (RGS) proteins constitutively activate Gbeta gamma-gated potassium channels.Expression levels of RGS7 and RGS4 proteins determine the mode of regulation of the G protein-activated K(+) channel and control regulation of RGS7 by G beta 5.Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to Gtpase-activating protein activity.Identification of effector residues on photoreceptor G protein, transducin.Immunohistochemical distribution of RGS7 protein and cellular selectivity in colocalizing with Galphaq proteins in the adult rat brain.RGS4 binds to membranes through an amphipathic alpha -helix.Regulation of transducin GTPase activity by human retinal RGS.

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P2860

The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.

http://www.wikidata.org/entity/Q36072644

description

1997 nî lūn-bûn

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年學術文章

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1997年學術文章

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1997年學術文章

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The core domain of a new retin ...... tivity of transducin in vitro.

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The core domain of a new retin ...... tivity of transducin in vitro.

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Proceedings of the National Academy of Sciences of the United States of America

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The core domain of a new retin ...... ctivity of transducin in vitro

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J B Hurley

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P2860

GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain

Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family

RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling

Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae

GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits

Basic local alignment search tool

Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone.

Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization, and genetic interaction and physical association with Gpa1 (the G-protein alpha subunit).

EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins

GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits

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