Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling

scientific article published in January 2004

Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling is …
instance of (P31):
scholarly articleQ13442814
review articleQ7318358

External links are
P356DOI10.1016/S0076-6879(04)89006-2
P698PubMed publication ID15313561

P2093author name stringYaping Tu
Thomas M Wilkie
P2860cites workCa2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activityQ22253430
RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of GzalphaQ24316172
The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitroQ24655997
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysisQ27736041
Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residueQ28138422
Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10Q28141136
GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteinsQ28145018
Palmitoylation regulates regulator of G-protein signaling (RGS) 16 function. II. Palmitoylation of a cysteine residue in the RGS box is critical for RGS16 GTPase accelerating activity and regulation of Gi-coupled signallingQ28184243
RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylationQ28198826
G proteins: transducers of receptor-generated signalsQ29547519
Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunitsQ34444567
Analyses of RGS protein control of agonist-evoked Ca2+ signalingQ35864203
Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-activating proteinsQ36424021
Regulators of G-protein signaling (RGS) 4, insertion into model membranes and inhibition of activity by phosphatidic acidQ38358455
Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to Gtpase-activating protein activityQ43556709
RGS4 binds to membranes through an amphipathic alpha -helix.Q52538794
Expression of G-protein alpha subunits in Escherichia coli.Q54645309
Purification of Recombinant G Proteins from Sf9 Cells by Hexahistidine Tagging of Associated SubunitsQ56593501
Dynamic Regulation of RGS2 Suggests a Novel Mechanism in G-Protein Signaling and Neuronal PlasticityQ61893595
Recognition and characterization of calmodulin-binding sequences in peptides and proteinsQ69032811
Mutational analysis of the Asn residue essential for RGS protein binding to G-proteinsQ74326003
The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signalingQ77696554
P407language of work or nameEnglishQ1860
P304page(s)89-105
P577publication date2004-01-01
P1433published inMethods in EnzymologyQ2076903
P1476titleAllosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling
P478volume389

Reverse relations

cites work (P2860)
Q42578482Evaluating modulators of "Regulator of G-protein Signaling" (RGS) proteins
Q41671424Functional cooperation of of IL-1β and RGS4 in the brachial plexus avulsion mediated brain reorganization
Q36061579G-protein signaling: back to the future
Q38978553Phosphatidic acid binding inhibits RGS1 activity to affect specific signaling pathways in Arabidopsis
Q57372759Regulation of RGS2 and Second Messenger Signaling in Vascular Smooth Muscle Cells by cGMP-dependent Protein Kinase
Q34198530Regulators of G-protein signaling and their Gα substrates: promises and challenges in their use as drug discovery targets
Q48160738Three regulators of G protein signaling differentially affect mating, morphology and virulence in the smut fungus Ustilago maydis.

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