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RAS guanyl releasing protein 2

The protein encoded by this gene is a brain-enriched nucleotide exchanged factor that contains an N-terminal GEF domain, 2 tandem repeats of EF-hand calcium-binding motifs, and a C-terminal diacylglycerol/phorbol ester-binding domain. This protein can activate small GTPases, including RAS and RAP1/RAS3. The nucleotide exchange activity of this protein can be stimulated by calcium and diacylglycerol. Three alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Rap1, GEF, OUT, RAP, P2Y12
Papers on CalDAG-GEFI
RAP1-GTPase signaling and platelet function.
Bergmeier et al., Chapel Hill, United States. In J Mol Med (berl), Jan 2016
Our recent studies demonstrate that the antagonistic balance between the RAP1 regulators, CalDAG-GEFI and RASA3, is critical for the modulation of platelet adhesiveness, both in circulation and at sites of vascular injury.
Update on the inherited platelet disorders.
Lambert, Philadelphia, United States. In Curr Opin Hematol, Sep 2015
RECENT FINDINGS: The description of novel mechanisms of disease including mutations in PRKACG, in a family with severe macrothrombocytopenia, RUNX1 and FLI1 mutations in patients with inherited mild platelet function disorders and CalDAG-GEFI resulting in a severe platelet bleeding phenotype show that there is still much to be learned from studying families and molecular sequencing of patients with well phenotyped platelet disorders.
Inherited disorders of platelet function: selected updates.
Nurden et al., Pessac, France. In J Thromb Haemost, Jun 2015
Next-generation sequencing technology (NGST), mainly exome sequencing, has highlighted genes responsible for defects in platelet secretion (NBEAL2, gray platelet syndrome), procoagulant activity (STIM1, Stormorken syndrome), and activation pathways (RASGRP2, CalDAG-GEFI deficiency and integrin dysfunction; PRKACG, cyclic adenosine monophosphate-dependent protein kinase deficiency).
RASA3 is a critical inhibitor of RAP1-dependent platelet activation.
Bergmeier et al., In J Clin Invest, Apr 2015
RAP1 activity in platelets is controlled by the GEF CalDAG-GEFI and an unknown regulator that operates downstream of the adenosine diphosphate (ADP) receptor, P2Y12, a target of antithrombotic therapy.
Mechanisms of interferon-γ production by neutrophils and its function during Streptococcus pneumoniae pneumonia.
Doerschuk et al., In Am J Respir Cell Mol Biol, Mar 2015
The guanine nucleotide exchange factor CalDAG-GEFI modulates IFN-γ production.
CLL2-1, a chemical derivative of orchid 1,4-phenanthrenequinones, inhibits human platelet aggregation through thiol modification of calcium-diacylglycerol guanine nucleotide exchange factor-I (CalDAG-GEFI).
Wu et al., Kao-hsiung, Taiwan. In Free Radic Biol Med, 2015
CalDAG-GEFI is a guanine nucleotide exchange factor, which actives small GTPase Rap1 and plays an important role in platelet aggregation.
CalDAG-GEFI deficiency protects mice from FcγRIIa-mediated thrombotic thrombocytopenia induced by CD40L and β2GPI immune complexes.
Bergmeier et al., Winter Park, United States. In J Thromb Haemost, 2014
Here we evaluated the contribution of the guanine nucleotide exchange factor, CalDAG-GEFI, and P2Y12, key regulators of Rap1 signaling in platelets, to ITT induced by these clinically relevant ICs.
Human CalDAG-GEFI gene (RASGRP2) mutation affects platelet function and causes severe bleeding.
Tregouet et al., Marseille, France. In J Exp Med, 2014
Using whole-exome sequencing, we identified the culprit mutation (cG742T) in the RAS guanyl-releasing protein-2 (RASGRP2) gene coding for calcium- and DAG-regulated guanine exchange factor-1 (CalDAG-GEFI).
Identification of CalDAG-GEFI as an intracellular target for the vicinal dithiol binding agent phenylarsine oxide in human platelets.
Wu et al., Kao-hsiung, Taiwan. In Thromb Haemost, 2014
CalDAG-GEFI, a guanine nucleotide exchange factor activating Rap1, is known to play a key role in Ca2+-dependent glycoprotein (GP)IIb/IIIa activation and platelet aggregation.
Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.
Gambaryan et al., Würzburg, Germany. In J Thromb Haemost, 2013
OBJECTIVE: To identify the PKA phosphorylation sites in calcium and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), the main GEF for Rap1b in platelets, and the effect of CalDAG-GEFI phosphorylation in Rap1b activation.
Phosphorylation of the guanine-nucleotide-exchange factor CalDAG-GEFI by protein kinase A regulates Ca(2+)-dependent activation of platelet Rap1b GTPase.
Torti et al., Pavia, Italy. In Biochem J, 2013
In the present study we demonstrate that the Ca2+-dependent exchange factor for Rap1b, CalDAG-GEFI (calcium and diacylglycerol-regulated guanine-nucleotide-exchange factor I), is a novel substrate for the cAMP-activated PKA (protein kinase A).
Relative contributions of stromal interaction molecule 1 and CalDAG-GEFI to calcium-dependent platelet activation and thrombosis.
Bergmeier et al., Philadelphia, United States. In J Thromb Haemost, 2011
(i) STIM1/SOCE is critical for procoagulant activity but not the proadhesive function of platelets; and (ii) at the site of vascular injury, STIM1 and CalDAG-GEFI are critical for the first wave of thrombin generation mediated by procoagulant platelets
CalDAG-GEFI deficiency protects mice in a novel model of Fcγ RIIA-mediated thrombosis and thrombocytopenia.
Bergmeier et al., Philadelphia, United States. In Blood, 2011
we evaluated the contribution of CalDAG-GEFI to platelet activation in a model of immune-mediated thrombocytopenia and thrombosis syndromes
The kinetics of αIIbβ3 activation determines the size and stability of thrombi in mice: implications for antiplatelet therapy.
Bergmeier et al., Philadelphia, United States. In Blood, 2011
Studies indicate that CalDAG-GEFI mediates the rapid but reversible activation of integrin alphaIIbbeta3, and the adenosine diphosphate receptor P2Y12 facilitates delayed but sustained integrin activation.
Integrin-independent role of CalDAG-GEFI in neutrophil chemotaxis.
Wagner et al., Boston, United States. In J Leukoc Biol, 2010
CalDAG-GEFI helps regulate neutrophil chemotaxis, independent of its established role in integrin activation, through a mechanism that involves actin cytoskeleton and cellular polarization.
Identification of the gene regulatory region in human rasgrp2 gene in vascular endothelial cells.
Hori et al., Kure, Japan. In Biol Pharm Bull, 2009
analyzed the 5'-flanking region of rasgrp2 gene by a luciferase assay, which revealed that not only a promoter but also silencer regions were present upstream of D1E, suggesting rasgrp2 expression is controlled by a combination of promotion and repression
CalDAG-GEFI and platelet activation.
Bergmeier et al., Philadelphia, United States. In Platelets, 2009
Here, we review recent findings, which (a) identified CalDAG-GEFI (RasGRP2) at the nexus of the rapid Ca(2+)-dependent platelet activation, (b) demonstrated a complex synergy between signaling provided by CalDAG-GEFI, protein kinase C and the Gi-coupled receptor for ADP, P2Y12, and (c) suggested CalDAG-GEFI as a novel target for anti-platelet therapy.
Novel molecules in calcium signaling in platelets.
Stefanini et al., Philadelphia, United States. In J Thromb Haemost, 2009
Here, we review recent findings, which identified CalDAG-GEFI as a critical Ca2+ sensor that links increases in intracellular Ca2+ to integrin activation, TxA2 formation, and granule release in stimulated platelets.
Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation.
Hogg et al., London, United Kingdom. In Nat Med, 2009
The LAD-III lesion has been attributed to a C --> A mutation in the gene encoding calcium and diacylglycerol guanine nucleotide exchange factor (CALDAGGEF1; official symbol RASGRP2) specifying the CALDAG-GEF1 protein, but we show that this change is not responsible for the LAD-III disorder.
CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation.
Graybiel et al., Cambridge, United States. In Nat Med, 2004
To gain insight into the signaling systems that may be regulated by CalDAG-GEF/RasGRP family members, we have focused on CalDAG-GEFI, which is expressed preferentially in the brain and blood.
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