Affinage

RAP2B

Ras-related protein Rap-2b · UniProt P61225

Length
183 aa
Mass
20.5 kDa
Annotated
2026-04-28
48 papers in source corpus 23 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAP2B is a Ras-family small GTPase that functions as a signaling switch in platelet activation, phospholipase C-ε regulation, cytoskeletal remodeling, and cell survival after DNA damage. In platelets, RAP2B is activated by thrombin, ADP (via P2Y12), and convulxin through PI3K- and Ca²⁺-dependent pathways, and translocates to the cytoskeleton in a glycoprotein IIb-IIIa– and FcγII receptor–dependent manner (PMID:8356055, PMID:8183895, PMID:10224142, PMID:15613030). GTP-loaded RAP2B directly binds and recruits PLC-ε to the plasma membrane downstream of both Gs-coupled receptors (via EPAC1) and EGF receptor (via RasGRP3/c-Src), stimulating IP3 production and intracellular Ca²⁺ release that feed into ERK1/2 signaling (PMID:11877431, PMID:15143162, PMID:26201295). Dual palmitoylation at Cys176/Cys177—reversed by the depalmitoylase ABHD17a under EGFR/PI3K control—directs RAP2B to lipid rafts and the plasma membrane, and is essential for its roles in platelet activation, cytoskeletal regulation via plectin interaction, and promotion of migration and metastasis in colorectal cancer (PMID:18582561, PMID:39277583, PMID:40223002). RAP2B is also a direct p53 transcriptional target that promotes cell survival after DNA damage (PMID:23535297).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1990 High

    Identification of RAP2B as a novel Ras-family GTPase in platelets established that a distinct small GTPase—not a substrate of cAMP-dependent kinase—operates in platelet signaling.

    Evidence cDNA library screening from human platelets, bacterial expression, GTP/GDP-binding assays

    PMID:2118346 PMID:2118648

    Open questions at the time
    • No effector or upstream regulator identified
    • Subcellular localization in platelets unknown
    • Biological function in platelets undetermined
  2. 1992 Medium

    Partial purification of a dedicated RAP2B-GAP from brain membranes demonstrated that RAP2B GTPase cycling is regulated by a specific, immunologically distinct GAP, not shared with RAP1 or RAS.

    Evidence Biochemical purification from bovine brain membranes, GTPase activity assay, immunoblotting

    PMID:1472043

    Open questions at the time
    • GAP identity not molecularly cloned
    • In vivo relevance not established
    • No confirmation in human tissue
  3. 1993 High

    Demonstrating that RAP2B translocates to the platelet cytoskeleton upon activation and that this requires glycoprotein IIb-IIIa–mediated fibrinogen binding linked RAP2B to integrin outside-in signaling and cytoskeletal reorganization, while CAAX-dependent membrane association was shown to be necessary for RAP2B function in Xenopus oocytes.

    Evidence Triton X-100 fractionation of activated platelets with antibody blocking; Xenopus oocyte microinjection with CAAX cysteine mutagenesis

    PMID:7684898 PMID:8356055

    Open questions at the time
    • Direct molecular link between RAP2B and cytoskeletal components unknown
    • GTP-loading status during translocation not measured
    • Signal upstream of integrin engagement not defined
  4. 1994 High

    Using Glanzmann's thrombasthenia patient platelets lacking glycoprotein IIb-IIIa provided genetic proof that integrin αIIbβ3 is required for RAP2B cytoskeletal translocation, solidifying the integrin dependency.

    Evidence Patient platelet fractionation, monoclonal antibody blocking

    PMID:8183895

    Open questions at the time
    • Whether RAP2B is active (GTP-loaded) during translocation unknown
    • Direct physical interaction between RAP2B and integrin not demonstrated
  5. 1999 High

    Identification of a second pathway—FcγII receptor–dependent tyrosine phosphorylation downstream of GP Ib/vWF engagement—showed that RAP2B cytoskeletal recruitment is not exclusively integrin-dependent and involves tyrosine kinase signaling.

    Evidence FcγII receptor and tyrosine kinase inhibitor blocking, cAMP elevation, Western blot fractionation

    PMID:10224142

    Open questions at the time
    • Identity of tyrosine kinase(s) phosphorylating downstream targets unknown
    • Whether RAP2B is a direct substrate of tyrosine phosphorylation untested
  6. 2002 High

    Discovery that RAP2B specifically mediates PLC-ε activation downstream of Gs-coupled receptors via EPAC1 identified the first effector pathway for RAP2B, distinguishing it functionally from RAP1A, RAP2A, and other small GTPases.

    Evidence Dominant-negative RAP2B, GTP-loading assays, adenylyl cyclase inhibitor, clostridial toxin inactivation in COS cells

    PMID:11877431

    Open questions at the time
    • Direct physical interaction between RAP2B and PLC-ε not yet shown
    • Physiological context beyond COS cells not established
  7. 2004 High

    Demonstration of direct RAP2B–PLC-ε binding and plasma membrane recruitment downstream of EGFR via RasGRP3/c-Src established the molecular mechanism by which RAP2B activates PLC-ε, and systematic dissection of RAP2B activation in platelets by thrombin, ADP, and convulxin defined the upstream signaling requirements (PI3K, Ca²⁺, PKC).

    Evidence Co-immunoprecipitation of RAP2B and PLC-ε, translocation assay, dominant-negative epistasis; RAL-GDS-RBD pull-down GTP-loading assay with pharmacological inhibitors in platelets

    PMID:15143162 PMID:15613030

    Open questions at the time
    • Structural basis of RAP2B–PLC-ε interaction unknown
    • Whether RAP2B–PLC-ε axis operates in platelets not shown
  8. 2008 High

    Identification of dual palmitoylation at Cys176/Cys177 as the determinant of lipid raft targeting—distinct from CAAX-dependent general membrane association—revealed a post-translational code that restricts RAP2B to specific membrane microdomains critical for agonist-induced activation.

    Evidence Metabolic [³H]palmitate labeling, C176S/C177S mutagenesis, lipid raft fractionation, cholesterol depletion in platelets and HEK293T

    PMID:18582561

    Open questions at the time
    • Identity of the palmitoyl transferase unknown
    • Whether raft localization is dynamically regulated during signaling not addressed
  9. 2013 High

    ChIP evidence that p53 directly binds the RAP2B promoter to induce its transcription after DNA damage, and that RAP2B knockdown sensitizes cells to apoptosis, established RAP2B as a p53-regulated pro-survival factor linking the DNA damage response to small GTPase signaling.

    Evidence Chromatin immunoprecipitation, siRNA knockdown, apoptosis assays with p53-dependent epistasis

    PMID:23535297

    Open questions at the time
    • Which RAP2B effector pathway mediates the survival signal unknown
    • Whether RAP2B induction is relevant in non-cancer p53-wild-type contexts not tested
  10. 2015 Medium

    Connecting RAP2B to Ca²⁺-dependent ERK1/2 activation in breast cancer and to CAAX-dependent inhibition of cell spreading via actin dynamics provided functional links between RAP2B's GTPase activity and downstream proliferation, migration, and cytoskeletal effects.

    Evidence Overexpression/knockdown with Ca²⁺ chelation and MEK inhibition; C180A mutagenesis with nocodazole-induced actin staining

    PMID:25762091 PMID:26201295

    Open questions at the time
    • Whether ERK1/2 activation is PLC-ε–dependent or independent not resolved
    • Direct cytoskeletal binding partner of RAP2B not identified at this point
  11. 2017 Medium

    Extension of RAP2B signaling to PI3K/AKT/VEGF-mediated angiogenesis and to p53-driven PLC-ε-IP3-Ca²⁺ suppression of autophagy broadened the effector landscape of RAP2B beyond PLC-ε and ERK.

    Evidence PI3K inhibitor with VEGF ELISA and HUVEC tube formation; IP3/Ca²⁺ measurements and LC3 blotting after RAP2B manipulation

    PMID:28691643 PMID:29029384

    Open questions at the time
    • Direct interaction between RAP2B and PI3K not demonstrated
    • Autophagy suppression assessed only by LC3 levels without autophagic flux assay
  12. 2019 Medium

    RAP2B was shown to be recruited to Coxiella replicative vacuoles where it inhibits membrane fusion in a CAAX-dependent manner, implicating it in host–pathogen membrane dynamics beyond classical signaling roles.

    Evidence Overexpression of wild-type vs. ΔAAX mutant, CRV fluorescence microscopy, VAMP7 Western blot

    PMID:30763357

    Open questions at the time
    • Whether RAP2B recruitment is a host defense or pathogen exploitation strategy unknown
    • Mechanism linking RAP2B to VAMP7 reduction not established
  13. 2024 High

    Identification of ABHD17a as the RAP2B depalmitoylase regulated by EGFR/PI3K-dependent phosphorylation completed the palmitoylation cycle and showed that dynamic palmitoylation controls RAP2B membrane localization and metastatic potential in colorectal cancer in vivo.

    Evidence ABHD17a knockdown/overexpression, C176/C177 mutagenesis, palmitoylation assay, blocking peptide, in vivo metastasis model

    PMID:39277583

    Open questions at the time
    • Palmitoyl acyltransferase(s) adding palmitate to RAP2B still unidentified
    • Whether ABHD17a regulation of RAP2B occurs in platelets not tested
  14. 2025 High

    Identification of plectin as a direct RAP2B interactor whose F-actin assembly activity is modulated by RAP2B, together with intestine-specific Rap2B knockout suppressing CRC, provided the first direct cytoskeletal binding partner for RAP2B and genetic loss-of-function evidence for its role in tumorigenesis.

    Evidence Co-immunoprecipitation of RAP2B–plectin, intestine-specific knockout mouse, F-actin assembly assays, in vivo tumor model

    PMID:40223002

    Open questions at the time
    • Whether RAP2B–plectin interaction is GTP-dependent not addressed
    • Structural basis of RAP2B–plectin binding unknown
    • Whether plectin mediates RAP2B's platelet cytoskeletal effects untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the identity of the palmitoyl acyltransferase(s) for RAP2B, the structural basis of its interactions with PLC-ε and plectin, whether the PLC-ε–IP3–Ca²⁺ axis operates in platelets, and whether RAP2B directly engages PI3K or NF-κB components.
  • Palmitoyl acyltransferase identity unknown
  • No structural model for RAP2B–effector complexes
  • PI3K and NF-κB pathway connections lack evidence of direct interaction

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 5 GO:0008092 cytoskeletal protein binding 3
Localization
GO:0005856 cytoskeleton 5 GO:0005886 plasma membrane 4 GO:0005829 cytosol 2
Pathway
R-HSA-109582 Hemostasis 5
Partners
ABHD17APLCE1PLECRAPGEF3RASGRP3

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 RAP2B was identified as a novel GTP-binding protein in human platelets, cloning from a platelet cDNA library. Bacterially expressed RAP2B binds both GTP and GDP in a Mg2+-dependent fashion with higher relative affinity for GTP than GDP, and is a ~22 kDa protein. Unlike the closely homologous RAP1A and RAP1B, RAP2B is not phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. cDNA library screening, bacterial expression, GTP-binding assay on blots, in vitro kinase assay Proceedings of the National Academy of Sciences of the United States of America High 2118346 2118648
1992 A GTPase-activating protein (GAP) for RAP2B was partially purified from bovine brain membranes. This RAP2B-GAP (~55 kDa) stimulates GTP hydrolysis by RAP2B and is immunologically distinct from RAP1-GAP and RAS-GAP. Partial protein purification, GTPase activity assay, immunoblotting with specific antibodies Biochemical and biophysical research communications Medium 1472043
1993 RAP2B associates with the platelet cytoskeleton upon platelet activation by thrombin, thromboxane analogue U46619, or thapsigargin. This translocation is dependent on platelet aggregation and requires fibrinogen binding to glycoprotein IIb-IIIa, as blocking fibrinogen binding completely prevents cytoskeletal incorporation of RAP2B. Triton X-100 fractionation, differential centrifugation, Western blot with specific antiserum, pharmacological inhibition Proceedings of the National Academy of Sciences of the United States of America High 8356055
1993 Microinjection of RAP2B protein or RNA into Xenopus oocytes causes rearrangement of pigment granules (mottling). This effect requires post-translational processing dependent on the C-terminal CAAX motif cysteine residue, as mutation of the CAAX cysteine to serine prevents membrane association and mottling. RAP2B associates with oocyte membranes in a CAAX-dependent manner. Microinjection into Xenopus oocytes, CAAX cysteine mutagenesis, membrane fractionation, in vitro transcription The Biochemical journal High 7684898
1994 RAP2B translocation to the platelet cytoskeleton requires agonist-induced actin polymerization and depends on glycoprotein IIb-IIIa. Monoclonal antibodies against glycoprotein IIb-IIIa block RAP2B cytoskeletal translocation, and platelets from Glanzmann's thrombasthenia patients (lacking glycoprotein IIb-IIIa) fail to incorporate RAP2B into the cytoskeleton. RAP2B and glycoprotein IIb-IIIa co-translocate simultaneously to the cytoskeleton in comparable amounts. Triton X-100 fractionation, monoclonal antibody blocking, patient platelets (Glanzmann's thrombasthenia), comparative immunoblotting Proceedings of the National Academy of Sciences of the United States of America High 8183895
1999 Von Willebrand factor (vWF) stimulation induces rapid translocation of RAP2B (and later RAP1B) to the platelet cytoskeleton via glycoprotein Ib engagement, requiring stirring (shear) but not integrin activation. This translocation is mediated by FcγII receptor-dependent protein tyrosine phosphorylation; blocking FcγII receptor or inhibiting tyrosine kinases (genistein) or elevating cAMP prevents RAP2B cytoskeletal association. Triton X-100 fractionation, monoclonal antibody blocking, kinase inhibition, cAMP-elevating agents, Western blot The Journal of biological chemistry High 10224142
2002 RAP2B mediates stimulation of phospholipase C-epsilon (PLC-ε) downstream of Gs-coupled receptors and cyclic AMP signaling. The M3 muscarinic acetylcholine receptor activates RAP2B (GTP loading), and this RAP2B activation is required for PLC-ε stimulation. Dominant-negative RAP2B (but not inactive RAC1, RAS, RalA, RAP1A, or RAP2A) suppresses M3 mAChR-mediated PLC stimulation. The effect is mediated through EPAC1 (a cAMP-regulated GEF for Rap GTPases) and Gαs. Dominant-negative expression, adenylyl cyclase inhibitor (dd-Ado), GTP-loading assay, overexpression of PLC isoforms and catalytically inactive mutants, clostridial toxin inactivation The Journal of biological chemistry High 11877431
2004 EGF receptor activates RAP2B via a pathway involving PLC-γ1-dependent Ca2+/diacylglycerol activation of the GEF RasGRP3, which is then tyrosine-phosphorylated by c-Src. Activated RAP2B (GTP-loaded) binds directly to PLC-ε and induces its translocation to the plasma membrane, stimulating PLC/Ca2+ signaling. Dominant-negative RAP2B blocks EGF-induced PLC-ε activation. Dominant-negative expression, GTP-loading assay, co-immunoprecipitation (Rap2B-PLC-ε binding), plasma membrane translocation assay, c-Src inhibition, PLC-γ1 lipase-inactive mutant, intracellular Ca2+ chelation Molecular and cellular biology High 15143162
2004 RAP2B is activated (GTP-loaded) in human platelets by thrombin, convulxin (GPVI ligand), and ADP (predominantly via P2Y12 receptor). Thrombin-induced RAP2B activation is partially dependent on secreted ADP, requires PI3K activity and intracellular Ca2+, but does not require thromboxane A2, cytoskeletal interaction, or integrin αIIbβ3 outside-in signaling. Convulxin-induced RAP2B activation additionally requires PKC. GTP-loading assay (pull-down with RAL-GDS-RBD), pharmacological inhibitors, ADP scavenging, specific receptor antagonists Journal of thrombosis and haemostasis High 15613030
2008 RAP2B (but not RAP1B) localizes to lipid rafts in human platelets and transfected HEK293T cells. About 20% of RAP2B constitutively associates with lipid rafts. Palmitoylation at Cys176 and Cys177 (in addition to CAAX-dependent prenylation) is required for lipid raft targeting; mutation of either Cys176 or Cys177 to serine prevents raft association without altering general membrane localization. Disruption of lipid raft association by cholesterol depletion significantly impairs agonist-induced RAP2B activation and platelet aggregation. Lipid raft fractionation, metabolic [3H]palmitate labeling, site-directed mutagenesis of Cys176/Cys177, cholesterol depletion, platelet aggregation assay, transfection in HEK293T cells Cellular signalling High 18582561
2013 RAP2B is a direct transcriptional target of p53. Upon DNA damage, p53 binds to the RAP2B promoter and activates its transcription. RAP2B promotes cell survival after DNA damage (pro-survival function), and siRNA-mediated knockdown of RAP2B sensitizes cells to DNA damage-induced apoptosis in a p53-dependent manner. Integrative genomic approach, chromatin immunoprecipitation (p53 binding to RAP2B promoter), siRNA knockdown, apoptosis assays, p53-dependent epistasis Cell cycle (Georgetown, Tex.) High 23535297
2015 RAP2B promotes breast cancer cell proliferation, migration, and invasion via a calcium-related ERK1/2 signaling pathway. RAP2B elevates intracellular calcium levels, which in turn promotes ERK1/2 phosphorylation. Calcium chelation (BAPTA/AM) or MEK inhibition (U0126) reverses RAP2B-induced ERK1/2 phosphorylation and the associated proliferative/migratory effects. siRNA knockdown, overexpression, CCK-8 assay, flow cytometry, transwell assay, Western blot, pharmacological inhibitors (BAPTA/AM, U0126) Scientific reports Medium 26201295
2015 RAP2B regulates the cytoskeleton and inhibits cell spreading. Overexpression of RAP2B (but not the C180A mutant) inhibits cell spreading by disrupting actin dynamics upon nocodazole treatment. RAP2B expression is induced by nocodazole in a p53-dependent manner, though RAP2B itself is not required for p53-dependent cell cycle arrest. Western blot, immunofluorescence staining, overexpression and CAAX-motif mutagenesis (C180A), siRNA knockdown, nocodazole treatment Journal of cancer research and clinical oncology Medium 25762091
2017 RAP2B promotes cell migration and invasion in prostate cancer through activation of focal adhesion kinase (FAK). Elevated RAP2B increases phosphorylation of FAK, and a FAK-specific inhibitor (PF-573228) abolishes RAP2B-induced FAK phosphorylation and migration/invasion effects. siRNA knockdown, overexpression, CCK-8, transwell assay, Western blot for p-FAK, pharmacological FAK inhibition, in vivo xenograft Medical oncology Medium 27154636
2017 RAP2B upregulates p53-mediated PLCε-IP3-Ca2+ signaling and inhibits autophagy. p53 increases intracellular IP3 and Ca2+ levels through its target gene Rap2B, and RAP2B decreases LC3 protein levels (autophagic flux marker), suggesting RAP2B suppresses starvation-triggered autophagy via the Rap2B-PLCε-IP3-Ca2+ pathway. Microarray identification of p53 targets, overexpression, siRNA knockdown, IP3/Ca2+ measurement, LC3 Western blot Oncotarget Medium 29029384
2017 RAP2B promotes angiogenesis in renal cell carcinoma through the PI3K/AKT/VEGF signaling pathway. RAP2B knockdown decreases VEGF expression and secretion; RAP2B-mediated VEGF upregulation and endothelial tube formation are suppressed by PI3K inhibition. Western blot, qPCR, ELISA for VEGF, HUVEC growth and tube formation assay, siRNA knockdown, PI3K inhibitor, in vivo xenograft Tumour biology Medium 28691643
2019 RAP2B promotes glioma cell adhesion, proliferation, migration, and invasion by regulating NF-κB signaling and expression of MMP-2 and MMP-9. Knockdown of RAP2B significantly reduces NF-κB, MMP-2, and MMP-9 protein levels in glioma cells. siRNA knockdown, CCK-8, cell attachment, transwell, wound-healing assay, Western blot for NF-κB/MMP-2/MMP-9 Journal of neuro-oncology Medium 30997639
2019 RAP2B is recruited to the Coxiella replicative vacuole (CRV) in infected cells. Overexpression of active RAP2B (wild-type) but not its inactive ΔAAX mutant inhibits CRV development and blocks both homotypic (early phagosome fusion with CRV) and heterotypic (endosome/lysosome fusion with CRV) fusion events. RAP2B overexpression decreases v-SNARE VAMP7 levels, suggesting impaired membrane fusion capacity. Overexpression of RAP2B wt vs. ΔAAX mutant, fluorescence microscopy of CRV, VAMP7 Western blot PloS one Medium 30763357
2024 RAP2B undergoes S-palmitoylation at C176/C177 that is required for its plasma membrane localization and promotion of cell migration and invasion in colorectal cancer, independent of proliferation. ABHD17a is identified as the depalmitoylating enzyme for RAP2B; ABHD17a activity alters RAP2B plasma membrane localization and inhibits cell migration. EGFR/PI3K signaling regulates RAP2B palmitoylation status by phosphorylating ABHD17a. A peptide blocking C176/C177 attenuates RAP2B palmitoylation, disrupts plasma membrane localization, and suppresses CRC metastasis in vivo. Palmitoylation assay, C176/C177 mutagenesis, ABHD17a knockdown/overexpression, subcellular fractionation, PI3K inhibition, ABHD17a phosphorylation assay, blocking peptide, in vivo metastasis model Cell death & disease High 39277583
2025 RAP2B interacts with plectin and enhances plectin expression, which in turn inhibits plectin-mediated F-actin assembly and drives intestinal cytoskeletal remodeling to promote colorectal cancer tumorigenesis. Intestine-specific knockout of Rap2B suppresses CRC initiation and progression in vivo, reducing metastatic potential. Intestine-specific knockout mouse model, co-immunoprecipitation (RAP2B-plectin interaction), F-actin assembly assays, tumor initiation/progression in vivo, Western blot Cell death & disease High 40223002
2009 RAP2B activates the NF-κB pathway when overexpressed in Rat1 cells, promoting transformation (focus formation). Reporter gene assay showed RAP2B activates NF-κB more than 3-fold over mock vector. Focus formation assay, NF-κB reporter gene assay, stable transfection Chinese journal of lung cancer Low 20719111
2024 RAP2B was identified as a putative interactor of the luteinizing hormone receptor (LHR) by APEX2 proximity proteomics, with RAP2B modulating both LHR signaling and post-endocytic trafficking. APEX2 proximity proteomics, quantitative multiplexed proteomics with temporal profiling bioRxiv (preprint)preprint Low bio_10.1101_2024.06.14.599010

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 Rap2B promotes proliferation, migration, and invasion of human breast cancer through calcium-related ERK1/2 signaling pathway. Scientific reports 73 26201295
1990 RAP2B: a RAS-related GTP-binding protein from platelets. Proceedings of the National Academy of Sciences of the United States of America 72 2118648
2015 miR-342-3p targets RAP2B to suppress proliferation and invasion of non-small cell lung cancer cells. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 67 25663460
2002 Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B. The Journal of biological chemistry 62 11877431
2021 Exosomes miR-22-3p Derived from Mesenchymal Stem Cells Suppress Colorectal Cancer Cell Proliferation and Invasion by Regulating RAP2B and PI3K/AKT Pathway. Journal of oncology 55 34239562
2017 Long Noncoding RNA XIST Promotes Osteosarcoma Progression by Targeting Ras-Related Protein RAP2B via miR-320b. Oncology research 53 28409547
2013 Rap2b, a novel p53 target, regulates p53-mediated pro-survival function. Cell cycle (Georgetown, Tex.) 48 23535297
1999 Rap1B and Rap2B translocation to the cytoskeleton by von Willebrand factor involves FcgammaII receptor-mediated protein tyrosine phosphorylation. The Journal of biological chemistry 46 10224142
2016 MiR-194 inhibits cell proliferation and invasion via repression of RAP2B in bladder cancer. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 44 27133066
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
1993 Association of the low molecular weight GTP-binding protein rap2B with the cytoskeleton during platelet aggregation. Proceedings of the National Academy of Sciences of the United States of America 43 8356055
2017 Rap2B promotes angiogenesis via PI3K/AKT/VEGF signaling pathway in human renal cell carcinoma. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 28 28691643
1994 Glycoprotein IIb-IIIa and the translocation of Rap2B to the platelet cytoskeleton. Proceedings of the National Academy of Sciences of the United States of America 28 8183895
2008 Targeting of the small GTPase Rap2b, but not Rap1b, to lipid rafts is promoted by palmitoylation at Cys176 and Cys177 and is required for efficient protein activation in human platelets. Cellular signalling 21 18582561
2019 MicroRNA-147b Promotes Proliferation and Invasion of Human Colorectal Cancer by Targeting RAS Oncogene Family (RAP2B). Pathobiology : journal of immunopathology, molecular and cellular biology 20 31121595
2016 Rap2B promotes cell proliferation, migration and invasion in prostate cancer. Medical oncology (Northwood, London, England) 18 27154636
2022 TMEM43 promotes pancreatic cancer progression by stabilizing PRPF3 and regulating RAP2B/ERK axis. Cellular & molecular biology letters 17 35260078
2014 Rap2B promotes migration and invasion of human suprarenal epithelioma. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 17 24951956
2017 Knockdown of Rap2B Inhibits the Proliferation and Invasion in Hepatocellular Carcinoma Cells. Oncology research 16 28081729
1990 Properties of the exchange rate of guanine nucleotides to the novel rap-2B protein. Biochemical and biophysical research communications 15 2118346
2016 Structure, functional regulation and signaling properties of Rap2B. Oncology letters 14 27073477
2015 Rap2b promotes proliferation, migration, and invasion of lung cancer cells. Journal of receptor and signal transduction research 14 26671640
2004 Activation of the small GTPase Rap2B in agonist-stimulated human platelets. Journal of thrombosis and haemostasis : JTH 14 15613030
2019 Rap2B promotes cell adhesion, proliferation, migration and invasion of human glioma. Journal of neuro-oncology 12 30997639
2017 Knockdown of Rap2B, a Ras Superfamily Protein, Inhibits Proliferation, Migration, and Invasion in Cervical Cancer Cells via Regulating the ERK1/2 Signaling Pathway. Oncology research 12 28390112
2016 Rap2B GTPase: structure, functions, and regulation. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 12 27012552
2024 Inhibiting S-palmitoylation arrests metastasis by relocating Rap2b from plasma membrane in colorectal cancer. Cell death & disease 11 39277583
2020 Rap2B knockdown suppresses malignant progression of hepatocellular carcinoma by inactivating the PTEN/PI3K/Akt and ERK1/2 pathways. Molecular and cellular biochemistry 11 32052247
2015 p53 target gene Rap2B regulates the cytoskeleton and inhibits cell spreading. Journal of cancer research and clinical oncology 11 25762091
2017 Rap2b siRNA significantly enhances the anticancer therapeutic efficacy of adriamycin in a gold nanoshell-based drug/gene co-delivery system. Oncotarget 10 28423503
2009 [Identification and Functional Analysis of A Novel Candidate Oncogene RAP2B in Lung Cancer.]. Zhongguo fei ai za zhi = Chinese journal of lung cancer 10 20719111
2021 Rap2B promotes the proliferation and migration of human glioma cells via activation of the ERK pathway. Oncology letters 9 33692846
2020 Long non-coding RNA CCAT1 promotes non-small cell lung cancer progression by regulating the miR-216a-5p/RAP2B axis. Experimental biology and medicine (Maywood, N.J.) 7 33023331
2020 Long non-coding RNA GHET1/miR-105/RAP2B axis regulates the progression of acute myeloid leukemia. Journal of Cancer 7 33123297
2019 The cAMP effectors, Rap2b and EPAC, are involved in the regulation of the development of the Coxiella burnetii containing vacuole by altering the fusogenic capacity of the vacuole. PloS one 7 30763357
2020 miR-205 Expression Elevated With EDS Treatment and Induced Leydig Cell Apoptosis by Targeting RAP2B via the PI3K/AKT Signaling Pathway. Frontiers in cell and developmental biology 6 32596241
2020 Long non-coding RNA SNHG6 promotes tumorigenesis in melanoma cells via the microRNA-101-3p/RAP2B axis. Oncology letters 6 33123239
2017 p53 upregulates PLCε-IP3-Ca2+ pathway and inhibits autophagy through its target gene Rap2B. Oncotarget 6 29029384
1993 Microinjection of Rap2B protein or RNA induces rearrangement of pigment granules in Xenopus oocytes. The Biochemical journal 6 7684898
2022 MiR-199a-3p Induces Mesenchymal to Epithelial Transition of Keratinocytes by Targeting RAP2B. International journal of molecular sciences 4 36499729
2010 [Effects of Rap2b gene on foci formation and wound-healing of NIH3T3 cells]. Wei sheng yan jiu = Journal of hygiene research 4 20726223
2015 Expression and DNA methylation status of the Rap2B gene in human bronchial epithelial cells treated by cigarette smoke condensate. Inhalation toxicology 2 26308105
2025 Rap2B drives tumorigenesis and progression of colorectal cancer through intestinal cytoskeleton remodeling. Cell death & disease 1 40223002
2023 Hsa_circ_0008035 Knockdown Inhibits Bladder Cancer Progression through miR-1184/RAP2B Axis. Urologia internationalis 1 36958293
1992 Partial purification of a GTPase-activating protein for rap2b from bovine brain membranes. Biochemical and biophysical research communications 1 1472043
2025 Rap2B-mediated reprogramming of the PI3K/AKT signaling axis drives resistance to cetuximab-targeted therapy in colorectal carcinoma. Biological procedures online 0 41094393
2024 [Retracted] Long non‑coding RNA SNHG6 promotes tumorigenesis in melanoma cells via the microRNA‑101‑3p/RAP2B axis. Oncology letters 0 38385110
2022 MicroRNA-708 suppresses the proliferation, migration, and invasion of human retinoblastoma cells by targeting RAP2B, a member of the RAS oncogene family. Acta biochimica Polonica 0 36444911