Affinage

RASGRP3

Ras guanyl-releasing protein 3 · UniProt Q8IV61

Length
690 aa
Mass
78.3 kDa
Annotated
2026-04-28
37 papers in source corpus 23 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RasGRP3 is a diacylglycerol (DAG)/phorbol ester–regulated guanine nucleotide exchange factor (GEF) that integrates lipid second-messenger signals into Ras-family GTPase activation across immune, endothelial, and epithelial cell types. It catalyzes GDP-to-GTP exchange on H-Ras, R-Ras, Rap1, and Rap2B, and is recruited to membranes via its C1 domain upon DAG or phorbol ester binding; full catalytic activation additionally requires PKC-mediated phosphorylation on Thr133, with PKCδ, PKCε, PKCθ, and PKCβ2 each capable of this modification (PMID:10835426, PMID:11221888, PMID:15657177, PMID:15213298, PMID:28486107). In B cells, RasGRP3 cooperates with RasGRP1 to drive BCR-induced Ras-ERK signaling and proliferation, and Rasgrp3-null mice display hypogammaglobulinemia; in macrophages, RasGRP3 instead preferentially activates Rap1 upon TLR stimulation to restrain pro-inflammatory cytokine output (PMID:16301621, PMID:25118589). RasGRP3 protein stability is controlled by ubiquitin-dependent degradation mediated by the E3 ligases UHRF1 and MID1, and in GNAQ/GNA11-mutant uveal melanoma RasGRP3 serves as the obligate link between constitutive Gαq signaling and MAPK pathway activation (PMID:28486107, PMID:29490280, PMID:41689678, PMID:36826998).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2000 High

    Establishing that RasGRP3 is a bona fide GEF with broad Ras-family substrate specificity resolved whether the CalDAG-GEFIII gene product had direct catalytic exchange activity and defined H-Ras, R-Ras, and Rap1 as its substrates.

    Evidence In vitro GEF assay measuring GDP/GTP exchange on purified GTPases, confirmed by transfection in 293T cells and PC12 differentiation

    PMID:10835426

    Open questions at the time
    • Relative substrate preference under physiological DAG concentrations unknown
    • No structural basis for multi-substrate recognition
  2. 2001 High

    Demonstrating that the C1 domain binds DAG/phorbol esters and drives membrane translocation established the activation mechanism linking receptor-generated DAG to RasGRP3 catalytic output.

    Evidence Phorbol ester binding assay, GFP-RasGRP3 live-cell imaging, Ras-GTP pull-down in HEK-293 cells

    PMID:11221888

    Open questions at the time
    • Contribution of EF-hand and PT domains to membrane targeting not fully dissected
    • Whether C1-domain lipid selectivity differs from PKC C1 domains was untested
  3. 2004 High

    Identification of Thr133 as the PKC phosphorylation site required for full RasGRP3 activation revealed a two-signal activation model: DAG recruits RasGRP3 to membranes, and PKC phosphorylation (by PKCθ, PKCβ2, or PKCδ) amplifies its GEF output.

    Evidence Mass spectrometry, Thr133Ala mutagenesis, in vitro kinase assays with multiple PKC isoforms, BCR stimulation in B cells, co-IP of PKCδ–RasGRP3

    PMID:15213298 PMID:15545601 PMID:15657177

    Open questions at the time
    • Structural mechanism by which Thr133 phosphorylation enhances catalysis is unknown
    • Relative contributions of individual PKC isoforms in different cell types not resolved
  4. 2004 High

    Showing that RasGRP3 activates Rap2B downstream of EGF/c-Src to drive PLCε translocation extended the signaling repertoire beyond Ras-ERK and linked RasGRP3 to calcium signaling cascades.

    Evidence Dominant-negative Rap2B, c-Src inhibition, Rap2B GTP-loading assay, Ca²⁺ measurement in HEK-293 cells

    PMID:15143162

    Open questions at the time
    • Whether this Rap2B–PLCε axis operates in primary cell types is untested
    • Tyrosine phosphorylation site on RasGRP3 by c-Src not mapped
  5. 2005 High

    Genetic studies in Rasgrp1/Rasgrp3 single- and double-knockout mice established that RasGRP3 maintains basal Ras-GTP in resting B cells, cooperates with RasGRP1 for BCR-induced ERK activation, and is required for normal immunoglobulin production.

    Evidence Single and double null mice, Ras-GTP pull-down, B cell proliferation, serum immunoglobulin measurement

    PMID:16301621

    Open questions at the time
    • Which immunoglobulin class-switch step is RasGRP3-dependent is not defined
    • Whether B cell developmental stages are differentially affected is unclear
  6. 2004 High

    Loss-of-function in the embryonic vasculature demonstrated a non-immune role for RasGRP3: it is required for phorbol ester–induced endothelial dysmorphogenesis and is upregulated by VEGF, establishing RasGRP3 as a vascular DAG effector.

    Evidence Gene-trap mouse model, in situ hybridization, ES cell–derived vascular morphogenesis assay

    PMID:15572660

    Open questions at the time
    • Downstream GTPase substrate (Ras vs. Rap1) mediating vascular phenotype not identified
    • Relationship to VEGF receptor signaling pathway not fully mapped
  7. 2006 High

    Discovery that dynein light chain 1 (DLC1) binds the C-terminal domain of RasGRP3 and controls its subcellular distribution revealed a cytoskeletal-dependent localization mechanism for this GEF.

    Evidence Yeast two-hybrid, in vitro pull-down, co-IP, fluorescence microscopy of truncation mutant

    PMID:17012239

    Open questions at the time
    • Functional consequence of DLC1 interaction on Ras/Rap activation not tested
    • Whether dynein motor activity is required for RasGRP3 transport unknown
  8. 2011 High

    Gain- and loss-of-function studies in prostate cancer and melanoma cells showed that RasGRP3 overexpression is sufficient to drive Ras-AKT/ERK signaling, proliferation, and tumorigenicity, positioning it as an oncogenic driver in non-immune cancers.

    Evidence siRNA knockdown and overexpression, Ras-GTP pull-down, soft agar assay, mouse xenograft in prostate cancer and melanoma models

    PMID:20876802 PMID:21602881

    Open questions at the time
    • Mechanism of RasGRP3 overexpression in these cancers (amplification, transcriptional, post-translational) not established
    • Whether RasGRP3 signals through Ras or Rap in these contexts is unresolved
  9. 2014 High

    CRISPR knockout in macrophages revealed that RasGRP3 preferentially activates Rap1 (not Ras) upon TLR stimulation and thereby dampens inflammatory cytokine production, establishing a substrate-selective anti-inflammatory role.

    Evidence CRISPR-Cas9 KO in RAW264.7, Rap1 activity assay, cytokine ELISA, DSS-colitis and collagen-induced arthritis mouse models

    PMID:25118589

    Open questions at the time
    • Mechanism determining Rap1 vs. Ras substrate selectivity in macrophages unknown
    • Cell-type–specific transcriptional regulation of RasGRP3 in myeloid lineage not characterized
  10. 2017 High

    Identification of RasGRP3 as the obligate link between oncogenic GNAQ/GNA11 and MAPK in uveal melanoma solved a long-standing question about how constitutive Gαq signals reach Ras, revealing dual activation by PKC phosphorylation and DAG-mediated membrane recruitment.

    Evidence siRNA/shRNA knockdown, PKC isoform–specific studies, Ras-GTP and ERK assays in multiple UM cell lines, patient tumor analysis; confirmed by GNA11Q209L transgenic mouse model

    PMID:28486107 PMID:29490280

    Open questions at the time
    • Whether pharmacological targeting of RasGRP3 C1 domain can suppress UM growth in vivo is untested
    • Structural basis for RasGRP3 selectivity by DAG-lactone agonists incompletely understood
  11. 2023 Medium

    Discovery that MID1 and UHRF1 are E3 ubiquitin ligases targeting RasGRP3 for proteasomal degradation established post-translational stability control as a key regulatory layer, with pathological stabilization occurring in NPM1-mutant AML.

    Evidence Co-IP, cycloheximide chase, Western blot for NPM1-mA/MID1/RasGRP3 axis in AML cells; co-IP and ubiquitination assay for UHRF1–RasGRP3 in endothelial cells and ApoE−/− mice

    PMID:36826998 PMID:41689678

    Open questions at the time
    • Ubiquitination sites on RasGRP3 not mapped
    • Relative contributions of MID1 vs. UHRF1 in different tissues unknown
    • Findings from single labs, independent replication pending

Open questions

Synthesis pass · forward-looking unresolved questions
  • A structural understanding of how DAG binding, Thr133 phosphorylation, and substrate selectivity are integrated within the RasGRP3 catalytic cycle, and the in vivo therapeutic potential of C1-domain–selective ligands, remain unresolved.
  • No crystal or cryo-EM structure of RasGRP3
  • In vivo efficacy of RasGRP3-selective DAG-lactones not demonstrated
  • Mechanism of Ras vs. Rap substrate selection in different cell types undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0008289 lipid binding 3
Localization
GO:0005886 plasma membrane 3 GO:0005829 cytosol 2
Pathway
R-HSA-162582 Signal Transduction 9 R-HSA-1643685 Disease 4 R-HSA-168256 Immune System 2
Partners
ACTR3DYNLL1MID1PRKCBPRKCDPRKCQRAP2BUHRF1

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 CalDAG-GEFIII (RasGRP3) functions as a guanine nucleotide exchange factor (GEF) with broad substrate specificity, directly catalyzing GDP-to-GTP exchange on Ha-Ras, R-Ras, and Rap1 in vitro and in cells, and activating ERK/MAPK signaling. In vitro GEF assay (GTP/GDP ratio measurement), transfection in 293T cells, PC12 neuronal differentiation assay The Journal of biological chemistry High 10835426
2001 RasGRP3 binds phorbol esters via its C1 domain in an anionic phospholipid-dependent manner, and phorbol ester or diacylglycerol (DAG) binding causes RasGRP3 translocation to the plasma membrane/perinuclear area and activates its Ras exchange activity in intact cells. Phorbol ester binding assay, GFP-RasGRP3 fluorescence microscopy, RasGTP pull-down, ERK phosphorylation assay in HEK-293 cells Cancer research High 11221888
2003 RasGRP3 is phosphorylated upon BCR stimulation coincident with Ras activation; PKC inhibition attenuates both RasGRP3 phosphorylation and Ras activation. PKC-theta and PKC-beta2 phosphorylate RasGRP3 in vitro, and a dominant-active PKC-theta enhances Ras-ERK signaling via RasGRP3 when co-expressed in HEK-293 cells. In vitro kinase assay with PKC-theta and PKC-beta2, co-expression with dominant-active PKC-theta, PKC inhibitor studies, membrane fractionation, Ras activation assay Blood High 12730099
2004 PKC phosphorylates RasGRP3 specifically on Thr133; the Thr133Ala substitution abolishes PKC-dependent phosphorylation in vitro and severely impairs RasGRP3-mediated Ras activation in vivo after BCR stimulation. PKC activity (conventional PKCs) is required for Thr133 phosphorylation and full Ras-ERK activation. Mass spectrometry to identify phosphorylation site, in vitro kinase assay, site-directed mutagenesis (Thr133Ala), antiphospho-peptide antibody, PKC inhibitors, BCR stimulation of B cells Blood High 15545601 15657177
2004 PKCdelta physically associates with RasGRP3 upon PMA treatment (co-immunoprecipitation, colocalization in perinuclear region) and phosphorylates RasGRP3 in vitro; a PKCdelta kinase-dead mutant blocks the PMA-induced mobility shift of RasGRP3. Co-immunoprecipitation, in vitro kinase assay, immunofluorescence colocalization, dominant-negative PKCdelta, rottlerin inhibitor Molecular pharmacology High 15213298
2004 RasGRP3 activates Rap2B, leading to Rap2B-dependent translocation of PLC-epsilon to the plasma membrane and PLC/Ca2+ signaling downstream of the EGF receptor. EGF induces tyrosine phosphorylation of RasGRP3 by c-Src, and c-Src inhibition blocks both Rap2B activation and PLC stimulation. Dominant-negative Rap2B expression, clostridial toxin inactivation, co-expression of RasGRP3, GTP-loading assay for Rap2B, c-Src inhibition, Ca2+ signaling measurement in HEK-293 cells Molecular and cellular biology High 15143162
2004 RasGRP3 is expressed in embryonic blood vessels and is specifically required for the aberrant endothelial morphogenesis induced by phorbol ester (PMA); RasGRP3 loss-of-function makes vessels refractory to PMA-induced dysmorphogenesis. RasGRP3 expression is upregulated by VEGF stimulation of endothelial cells. ES cell gene trap screen, in situ hybridization, loss-of-function mouse model, ES cell-derived vascular morphogenesis assay Molecular and cellular biology High 15572660
2005 Both RasGRP1 and RasGRP3 contribute to BCR-induced Ras and ERK activation in B cells; RasGRP3 alone maintains basal Ras-GTP levels in resting B cells. Loss of RasGRP3 causes isotype-specific antibody deficiencies and hypogammaglobulinemia. BCR-induced B cell proliferation is RasGRP1- and RasGRP3-dependent. Single and double null mutant mice (Rasgrp1-/-, Rasgrp3-/-, double KO), Ras-GTP pull-down, ERK phosphorylation, B cell proliferation assays, serum immunoglobulin measurement Journal of immunology High 16301621
2005 Fluorescent phorbol esters induce translocation of RasGRP3 to intracellular membranes (primarily perinuclear/intracellular), and RasGRP3 colocalizes with the fluorescent phorbol ester. The lipophilicity of the phorbol ester determines kinetics and pattern of RasGRP3 redistribution. Fluorescent phorbol ester live-cell imaging, GFP-RasGRP3 fusion protein colocalization in CHO cells Molecular cancer therapeutics Medium 15657361
2005 RasGRP3 mediates phorbol ester-induced exocytosis in a PKC-independent manner; RasGRP3 is expressed in endocrine tissues and its effects on exocytosis are not blocked by MEK inhibitor but are partially sensitive to PKC inhibitor. Exocytosis assay in endocrine cells, PKC inhibitor, MEK inhibitor, ERK phosphorylation readout Biochemical and biophysical research communications Medium 15737652
2006 RasGRP3 interacts with dynein light chain 1 (DLC1) through its C-terminal 127 amino acids; this interaction was confirmed in vitro and by co-immunoprecipitation. Deletion of the C-terminal domain abolishes DLC1 interaction and dramatically alters RasGRP3 subcellular localization (strong reticular/perinuclear/nuclear distribution). Yeast two-hybrid screen, in vitro pull-down, co-immunoprecipitation, subcellular localization of truncation mutant (fluorescence microscopy) The Journal of biological chemistry High 17012239
2010 RasGRP3 is required for Ras-GTP formation, AKT and ERK1/2 phosphorylation, cell proliferation, migration, and anchorage-independent growth in prostate cancer cells. RasGRP3 overexpression in LNCaP cells elevates Ras-GTP, stimulates proliferation, and confers resistance to PMA-induced apoptosis. siRNA knockdown and overexpression, Ras-GTP pull-down, AKT/ERK phosphorylation, proliferation assay, migration assay, mouse xenograft Cancer research High 20876802
2011 RasGRP3 is required for Ras-GTP formation, Akt phosphorylation, c-Met expression, and cell proliferation/transformation in human melanoma cells. Overexpression of RasGRP3 in primary melanocytes alters morphology and induces tumorigenicity in mouse xenografts. siRNA knockdown, overexpression in primary melanocytes, Ras-GTP pull-down, Akt phosphorylation, soft agar colony formation, mouse xenograft Oncogene High 21602881
2011 RasGRP3 in endothelial cells promotes Ras-ERK signaling and endothelin-1-stimulated cell migration; Rasgrp3 loss-of-function attenuates Ras-ERK signaling and abolishes endothelin-1-induced migration, and embryos lacking Rasgrp3 are dramatically protected from diabetes-induced vascular developmental defects. Loss-of-function mouse model (Rasgrp3 null), endothelial cell migration assay, Ras-ERK signaling measurement, diabetic mouse model, primary endothelial cells with activated RasGRP3 Circulation research High 21474816
2014 RasGRP3 activates Rap1 upon low-level TLR stimulation in macrophages, which limits production of pro-inflammatory cytokines (especially IL-6). CRISPR-Cas9 deletion of RasGRP3 in RAW264.7 cells inhibits TLR3/4/9-induced Rap1 activation while enhancing ERK1/2 activation and IL-6 production. CRISPR-Cas9 knockout in RAW264.7, Rap1 activity assay, ERK1/2 phosphorylation, cytokine ELISA, DSS-colitis and collagen-induced arthritis mouse models Nature communications High 25118589
2015 RasGRP3 interacts with Arp3 (actin-related protein), as identified by pull-down/mass spectrometry and confirmed by co-immunoprecipitation and immunofluorescence. PMA-induced translocation of RasGRP3 increases its association with Arp3. Arp3 silencing partially reduces RasGRP3-mediated glioma cell migration. Pull-down assay with mass spectrometry, co-immunoprecipitation, immunofluorescence colocalization, siRNA knockdown of Arp3, migration assay Oncotarget Medium 25682201
2017 In GNAQ-mutant uveal melanoma, RasGRP3 is phosphorylated and activated by PKC-delta and PKC-epsilon, enabling Ras-MAPK pathway activation. RasGRP3 activation also occurs through PKC-independent DAG-mediated membrane recruitment. RasGRP3 knockdown suppresses MAPK activation, identifying RasGRP3 as the mechanistic link between Gαq signaling and MAPK in uveal melanoma. Knockdown (siRNA/shRNA), PKC isoform-specific studies, Ras-GTP assay, ERK phosphorylation, membrane fractionation, uveal melanoma cell lines and patient samples Cancer cell High 28486107
2018 In a GNA11Q209L mouse model, RasGRP3 is specifically required for GNAQ/GNA11-driven Ras activation and tumorigenesis; integrative transcriptome analysis identified RasGRP3 as selectively expressed in Gq-driven melanomas, and its loss suppresses tumor formation. Transgenic GNA11Q209L mouse model, Bap1 conditional KO, integrative transcriptome analysis, RasGRP3 knockdown in human UM cell lines, Ras activation assay, in vivo tumor models Cell reports High 29490280
2018 Alpha-arylidene DAG-lactones can selectively bind the RasGRP3 C1 domain with up to 73-fold selectivity over PKCα and 45-fold over PKCε in vitro, and selectively activate Ras (via RasGRP3) over PKCδ phosphorylation in intact cells. In vitro C1-domain binding assay (competitive displacement), intact cell Ras activation assay, PKCδ phosphorylation assay Journal of medicinal chemistry Medium 29860841
2023 In NPM1-mutant AML, cytoplasmic NPM1-mA binds E3 ubiquitin ligase MID1, blocking MID1-mediated degradation of RasGRP3 and thus stabilizing RasGRP3 protein. Stabilized RasGRP3 activates the EGFR-STAT3 axis to promote AML cell proliferation and autophagy. Co-immunoprecipitation, Western blot, cycloheximide chase assay, CCK8, EdU staining, immunofluorescence Journal of leukocyte biology Medium 36826998
2023 AC092894.1 lncRNA acts as a scaffold mediating USP3-dependent de-ubiquitination of AR, which then drives transcription of RASGRP3 to sustain MAPK signaling in colorectal cancer cells; loss of this axis promotes oxaliplatin resistance. RNA pull-down, RIP, co-immunoprecipitation, gain/loss-of-function experiments, in vivo mouse model BMC medicine Medium 37013584
2026 RasGRP3 promotes RAP1B GTP-loading (exchange factor activity) in endothelial cells, thereby inhibiting NF-κB pathway activation and reducing pro-inflammatory cytokine production and monocyte adhesion. UHRF1 (E3 ubiquitin ligase) binds RasGRP3 and promotes its ubiquitination and degradation; UHRF1 knockdown increases RasGRP3 protein levels. RasGRP3 overexpression in endothelial cells and ApoE-/- mice, RAP1 activity assay, NF-κB pathway assay, cytokine ELISA, THP-1 adhesion assay, co-immunoprecipitation for UHRF1-RasGRP3 interaction Inflammation Medium 41689678

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 RasGRP3 Mediates MAPK Pathway Activation in GNAQ Mutant Uveal Melanoma. Cancer cell 129 28486107
2000 CalDAG-GEFIII activation of Ras, R-ras, and Rap1. The Journal of biological chemistry 124 10835426
2005 RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling. Journal of immunology (Baltimore, Md. : 1950) 111 16301621
2003 Integration of DAG signaling systems mediated by PKC-dependent phosphorylation of RasGRP3. Blood 104 12730099
2001 Phorbol esters modulate the Ras exchange factor RasGRP3. Cancer research 90 11221888
2005 Phosphorylation of RasGRP3 on threonine 133 provides a mechanistic link between PKC and Ras signaling systems in B cells. Blood 86 15657177
2018 GNA11 Q209L Mouse Model Reveals RasGRP3 as an Essential Signaling Node in Uveal Melanoma. Cell reports 69 29490280
2004 Activation of RasGRP3 by phosphorylation of Thr-133 is required for B cell receptor-mediated Ras activation. Proceedings of the National Academy of Sciences of the United States of America 65 15545601
2016 GRP-3 and KAPP, encoding interactors of WAK1, negatively affect defense responses induced by oligogalacturonides and local response to wounding. Journal of experimental botany 64 26748394
2014 RasGRP3 limits Toll-like receptor-triggered inflammatory response in macrophages by activating Rap1 small GTPase. Nature communications 50 25118589
2004 Rap2B-dependent stimulation of phospholipase C-epsilon by epidermal growth factor receptor mediated by c-Src phosphorylation of RasGRP3. Molecular and cellular biology 44 15143162
2004 A vascular gene trap screen defines RasGRP3 as an angiogenesis-regulated gene required for the endothelial response to phorbol esters. Molecular and cellular biology 42 15572660
2010 RasGRP3 contributes to formation and maintenance of the prostate cancer phenotype. Cancer research 40 20876802
2004 PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters. Molecular pharmacology 39 15213298
2011 RasGRP3, a Ras activator, contributes to signaling and the tumorigenic phenotype in human melanoma. Oncogene 33 21602881
2023 Downregulation of AC092894.1 promotes oxaliplatin resistance in colorectal cancer via the USP3/AR/RASGRP3 axis. BMC medicine 27 37013584
2005 Role of phorbol ester localization in determining protein kinase C or RasGRP3 translocation: real-time analysis using fluorescent ligands and proteins. Molecular cancer therapeutics 27 15657361
2014 Function of RasGRP3 in the formation and progression of human breast cancer. Molecular cancer 22 24779681
1995 The nodule-specific VfENOD-GRP3 gene encoding a glycine-rich early nodulin is located on chromosome I of Vicia faba L. and is predominantly expressed in the interzone II-III of root nodules. Plant molecular biology 20 7632912
2015 Dysregulation of RasGRP1 in rheumatoid arthritis and modulation of RasGRP3 as a biomarker of TNFα inhibitors. Arthritis research & therapy 18 26714738
2006 The exchange factor and diacylglycerol receptor RasGRP3 interacts with dynein light chain 1 through its C-terminal domain. The Journal of biological chemistry 18 17012239
2011 The Ras activator RasGRP3 mediates diabetes-induced embryonic defects and affects endothelial cell migration. Circulation research 17 21474816
2015 RasGRP3 regulates the migration of glioma cells via interaction with Arp3. Oncotarget 16 25682201
2017 RasGRP3 controls cell proliferation and migration in papillary thyroid cancer by regulating the Akt-MDM2 pathway. Gene 15 28864115
2014 Upregulation of RASGRP3 expression in prostate cancer correlates with aggressive capabilities and predicts biochemical recurrence after radical prostatectomy. Prostate cancer and prostatic diseases 13 24418912
2013 RasGRP1, but not RasGRP3, is required for efficient thymic β-selection and ERK activation downstream of CXCR4. PloS one 13 23308188
2016 RasGRP1 and RasGRP3 Are Required for Efficient Generation of Early Thymic Progenitors. Journal of immunology (Baltimore, Md. : 1950) 12 27465532
2005 RasGRP3 mediates phorbol ester-induced, protein kinase C-independent exocytosis. Biochemical and biophysical research communications 10 15737652
2018 A somatic mutation of RasGRP3 decreases Na+/I- symporter expression in metastases of radioactive iodine-refractory thyroid cancer by stimulating the Akt signaling pathway. American journal of cancer research 9 30323976
2023 Mutant NPM1 maintains RASGRP3 protein stability via interaction with MID1 to promote acute myeloid leukemia cell proliferation and autophagy. Journal of leukocyte biology 6 36826998
2018 α-Arylidene Diacylglycerol-Lactones (DAG-Lactones) as Selective Ras Guanine-Releasing Protein 3 (RasGRP3) Ligands. Journal of medicinal chemistry 6 29860841
2018 RasGRP3, a Ras guanyl releasing protein 3 that contributes to malignant proliferation and aggressiveness in human esophageal squamous cell carcinoma. Clinical and experimental pharmacology & physiology 5 29461644
2023 Citri Reticulatae Pericarpium Limits TLR-4-Triggered Inflammatory Response in Raw264.7 Macrophages by Activating RasGRP3. International journal of molecular sciences 4 37762079
2019 RasGRP3 in peripheral blood mononuclear cells is associated with disease activity and implicated in the development of systemic lupus erythematosus. American journal of translational research 4 30972203
2017 The Effects of Low Doses of Gamma-Radiation on Growth and Membrane Activity of Pseudomonas aeruginosa GRP3 and Escherichia coli M17. Cell biochemistry and biophysics 4 29039057
2017 Novel transduction of nutrient stress to Notch pathway by RasGRP3 promotes malignant aggressiveness in human esophageal squamous cell carcinoma. Oncology reports 3 29048643
2026 RasGRP3 Promotes RAP1B Activity to Inhibit Endothelial Inflammation and Alleviate Atherosclerosis in High-Fat Diet-Fed ApoE-/- Mice. Inflammation 0 41689678