Affinage

RAP2B

Ras-related protein Rap-2b · UniProt P61225

Length
183 aa
Mass
20.5 kDa
Annotated
2026-06-10
48 papers in source corpus 23 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAP2B is a Ras-family small GTPase, originally characterized in human platelets, that cycles between GDP- and GTP-bound states and binds guanine nucleotides in a Mg2+-dependent manner with preference for GTP (PMID:2118648, PMID:2118346). Its membrane targeting depends on two layers of C-terminal processing: CAAX-motif prenylation, which is required for membrane association and downstream cellular effects (PMID:7684898, PMID:25762091), and S-palmitoylation at Cys176/Cys177, which directs RAP2B to lipid rafts and the plasma membrane; this palmitoylation cycle is controlled by the depalmitoylase ABHD17a under EGFR/PI3K regulation (PMID:18582561, PMID:39277583). RAP2B is loaded with GTP downstream of diverse receptors — GPCRs via a cAMP/Epac1 route from the M3 muscarinic receptor, the EGF receptor via c-Src-dependent phosphorylation of the GEF RasGRP3, and platelet receptors (GPCRs/P2Y12, GPVI, and the GPIb–FcγRII–Syk axis) (PMID:11877431, PMID:15143162, PMID:15613030, PMID:10224142). A central effector function is direct binding to phospholipase C-ε and driving its translocation to the plasma membrane, thereby stimulating IP3/Ca2+ signaling (PMID:15143162). During platelet aggregation RAP2B translocates to the cytoskeleton in a manner dependent on actin polymerization and fibrinogen binding to glycoprotein IIb-IIIa (PMID:8356055, PMID:8183895). RAP2B is a direct transcriptional target of p53 that promotes survival after DNA damage and suppresses starvation-induced autophagy through the PLC-ε–IP3–Ca2+ axis (PMID:23535297, PMID:29029384). In multiple cancers RAP2B drives proliferation, migration, invasion, and angiogenesis through Ca2+/ERK1/2, PI3K/AKT (including VEGF induction and cetuximab resistance), FAK, and NF-κB signaling (PMID:26201295, PMID:28691643, PMID:27154636, PMID:30997639, PMID:41094393), and it remodels the cytoskeleton by interacting with plectin to modulate F-actin assembly (PMID:40223002).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1990 High

    Established that RAP2B is a genuine GTP-binding protein distinct from the related RAP1 proteins, defining it as a candidate signaling GTPase in platelets.

    Evidence cDNA cloning, bacterial expression, GTP-blotting and kinase assay; in vitro GTP/GDP binding and immunoprecipitation from platelet membranes

    PMID:2118346 PMID:2118648

    Open questions at the time
    • No physiological GEF or receptor input identified at this stage
    • Cellular function unknown
  2. 1992 Medium

    Identified a RAP2-subfamily-specific GAP, addressing how RAP2B is switched off and distinguishing its regulation from RAP1/RAS.

    Evidence Partial protein purification from bovine brain membranes with GTPase assays and antibody discrimination

    PMID:1472043

    Open questions at the time
    • GAP protein not molecularly identified or cloned
    • Single lab, partially purified material
  3. 1993 High

    Linked RAP2B to cytoskeletal dynamics by showing it translocates to the cytoskeleton on platelet activation and induces cytoskeleton-dependent rearrangements requiring CAAX processing.

    Evidence Platelet subcellular fractionation with multiple agonists; Xenopus oocyte microinjection with CAAX mutagenesis and phalloidin block

    PMID:7684898 PMID:8356055

    Open questions at the time
    • Molecular effectors of cytoskeletal effect not identified
    • Direct cytoskeletal binding partner unknown
  4. 1994 High

    Defined the receptor requirement for cytoskeletal translocation, showing it depends on GPIIb-IIIa and actin polymerization, using genetic (Glanzmann) evidence.

    Evidence Platelet fractionation with blocking antibodies and Glanzmann thrombasthenia patient platelets

    PMID:8183895

    Open questions at the time
    • Mechanistic link between GPIIb-IIIa engagement and RAP2B recruitment unresolved
  5. 1999 High

    Mapped a distinct receptor pathway (vWF/GPIb–FcγRII–Syk) driving RAP2B cytoskeletal translocation, broadening the upstream signaling inputs.

    Evidence Platelet fractionation with receptor-blocking antibodies, tyrosine kinase inhibitors, and substrate identification

    PMID:10224142

    Open questions at the time
    • Direct GEF connecting Syk signaling to RAP2B not identified
  6. 2002 High

    Identified PLC-ε as a RAP2B effector and an Epac1/cAMP route for its activation, establishing RAP2B as a specific transducer to Ca2+ signaling downstream of GPCRs.

    Evidence Dominant-negative and toxin tools, GTP-loading and PLC/Ca2+ assays in HEK-293 cells with multi-GTPase specificity controls

    PMID:11877431

    Open questions at the time
    • Direct RAP2B–PLC-ε binding not yet demonstrated at this stage
  7. 2004 High

    Demonstrated direct RAP2B–PLC-ε binding and PLC-ε translocation, and placed RAP2B downstream of EGFR via c-Src/RasGRP3, providing the core effector mechanism.

    Evidence Co-IP, confocal translocation imaging, GTP-loading, dominant-negative and c-Src inhibition in HEK-293; GTP-loading assays in platelets dissecting thrombin vs convulxin inputs

    PMID:15143162 PMID:15613030

    Open questions at the time
    • Structural basis of RAP2B–PLC-ε interaction unknown
    • GEF identity in platelet pathways not resolved
  8. 2008 High

    Showed that palmitoylation at Cys176/Cys177 targets RAP2B to lipid rafts and is required for its agonist-induced activation, defining a membrane-microdomain control point.

    Evidence Detergent-resistant membrane fractionation, [3H]palmitate labeling, mutagenesis, cholesterol depletion, and aggregation assays in platelets and HEK293T

    PMID:18582561

    Open questions at the time
    • Enzymes controlling the palmitoylation cycle not yet identified
  9. 2013 High

    Placed RAP2B in the p53 network as a direct transcriptional target mediating survival after DNA damage, connecting it to tumor-relevant signaling.

    Evidence ChIP for p53 binding to the RAP2B promoter plus siRNA knockdown and apoptosis assays with p53-dependency controls

    PMID:23535297

    Open questions at the time
    • Downstream survival effectors of RAP2B in this context not defined
  10. 2017 Medium

    Connected the p53–RAP2B axis to autophagy, showing RAP2B mediates p53-dependent autophagy inhibition through PLC-ε–IP3–Ca2+.

    Evidence Microarray target identification, overexpression/knockdown, and measurement of IP3, Ca2+, and LC3

    PMID:29029384

    Open questions at the time
    • Single lab
    • Link to canonical autophagy machinery beyond LC3 not detailed
  11. 2019 Medium

    Extended RAP2B function to membrane trafficking, showing active RAP2B impairs Coxiella vacuole biogenesis and reduces the v-SNARE Vamp7.

    Evidence WT vs inactive ΔAAX mutant overexpression, vacuole imaging, fusion assays, and Vamp7 immunoblot

    PMID:30763357

    Open questions at the time
    • Mechanism linking RAP2B to Vamp7 levels unclear
    • Physiological (non-infection) trafficking role untested
  12. 2024 High

    Resolved the regulated palmitoylation cycle, identifying ABHD17a as the RAP2B depalmitoylase under EGFR/PI3K control and showing membrane targeting drives metastasis.

    Evidence Mutagenesis, palmitoylation assays, Co-IP of ABHD17a, PI3K inhibition, blocking peptide, and xenograft metastasis model

    PMID:39277583

    Open questions at the time
    • Palmitoyl-acyltransferase that adds the modification not identified
  13. 2025 High

    Provided in vivo genetic proof that RAP2B drives colorectal tumorigenesis and identified plectin as a binding partner mediating its cytoskeletal effects, while reinforcing PI3K/AKT-dependent therapy resistance.

    Evidence Intestine-specific knockout mice, Co-IP of RAP2B–plectin, F-actin readouts, metastasis assays; bidirectional manipulation with PI3K/AKT readout and cetuximab-resistance xenografts

    PMID:40223002 PMID:41094393

    Open questions at the time
    • How RAP2B nucleotide state controls plectin binding/F-actin is undefined
    • Relation between plectin axis and PLC-ε/Ca2+ signaling unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • The integrated upstream GEF network and the structural/nucleotide-state logic coupling RAP2B to its distinct effectors (PLC-ε, plectin, SNARE machinery) across cell types remain unresolved.
  • No unified model of which GEF acts in which receptor context
  • No structural data on effector selection
  • Tissue-specific GAP regulation uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 4 GO:0060089 molecular transducer activity 3 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0005886 plasma membrane 3 GO:0005856 cytoskeleton 2 GO:0005829 cytosol 1
Pathway
R-HSA-1643685 Disease 5 R-HSA-109582 Hemostasis 4 R-HSA-162582 Signal Transduction 4 R-HSA-9612973 Autophagy 1
Partners
ABHD17AITGB3PLCE1PLECRASGRP3

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 RAP2B encodes a ~22 kDa GTP-binding protein expressed in human platelets; bacterially expressed RAP2B specifically binds GTP on blots, and unlike RAP1A/RAP1B it is not phosphorylated by the catalytic subunit of cAMP-dependent protein kinase. cDNA cloning, bacterial expression, GTP-blotting, in vitro kinase assay Proceedings of the National Academy of Sciences of the United States of America High 2118648
1990 Purified recombinant RAP2B binds both GTP and GDP in a Mg2+-dependent fashion, with higher relative affinity for GTP than GDP; a polyclonal antiserum against recombinant RAP2B recognizes a ~21 kDa protein in platelet membrane fractions and immunoprecipitates RAP2B complexed with GTP or GDP. In vitro GTP/GDP binding assay, immunoprecipitation, Western blot Biochemical and biophysical research communications High 2118346
1992 A partially purified protein from bovine brain membranes stimulates the GTPase activity of RAP2B (a RAP2B-GAP); this GAP activity is immunologically distinct from RAP1-GAP and RAS-GAP, yet shows limited stimulatory activity toward RAP1, indicating it is a distinct GAP for the RAP2 subfamily. Partial protein purification from bovine brain membranes, GTPase activity assay, immunoblotting with specific antibodies Biochemical and biophysical research communications Medium 1472043
1993 RAP2B translocates from the Triton X-100-soluble fraction to the cytoskeleton upon platelet aggregation induced by thrombin, thromboxane analogue, or thapsigargin; translocation depends on platelet aggregation and requires fibrinogen binding to glycoprotein IIb-IIIa. Subcellular fractionation (Triton X-100 lysis, differential centrifugation), Western blot with specific antiserum Proceedings of the National Academy of Sciences of the United States of America High 8356055
1993 Microinjection of RAP2B protein or mRNA into Xenopus oocytes induces rearrangement of pigment granules ('mottling'); this effect requires membrane association via post-translational processing of the C-terminal CAAX motif, as a Cys→Ser mutation in the CAAX box prevents membrane association and mottling. The effect is blocked by the cytoskeletal reagent phalloidin. Xenopus oocyte microinjection, site-directed mutagenesis, membrane fractionation The Biochemical journal High 7684898
1994 Translocation of RAP2B to the platelet cytoskeleton requires agonist-induced actin polymerization and is dependent on glycoprotein IIb-IIIa (the fibrinogen receptor); platelets from Glanzmann thrombasthenia patients lacking GPIIb-IIIa fail to incorporate RAP2B into the cytoskeleton. RAP2B and GPIIb-IIIa co-translocate to the cytoskeleton during aggregation. Platelet fractionation, blocking antibodies against GPIIb-IIIa, use of Glanzmann thrombasthenia patient platelets, Western blot Proceedings of the National Academy of Sciences of the United States of America High 8183895
1999 von Willebrand factor (vWF) stimulation of human platelets induces rapid translocation of RAP2B to the cytoskeleton via a pathway requiring GPIb, FcγRII receptor-mediated tyrosine phosphorylation, and the kinase pp72(syk); translocation is blocked by genistein (tyrosine kinase inhibitor), cAMP-elevating agents, and anti-FcγRII antibody. Platelet fractionation, blocking antibodies (anti-GPIb, anti-FcγRII, RGDS peptide), pharmacological inhibitors (genistein, cytochalasin D, cAMP agents), Western blot, identification of substrates (syk, PLCγ2, SHIP) The Journal of biological chemistry High 10224142
2002 RAP2B mediates stimulation of phospholipase C-epsilon (PLC-ε) downstream of the M3 muscarinic acetylcholine receptor; this occurs via a cAMP/Epac1 pathway: M3 mAChR activates adenylyl cyclase, raises cAMP, activates Epac1 (a Rap GEF), which loads GTP onto RAP2B, which then stimulates PLC-ε to increase [Ca2+]i. Dominant-negative RAP2B (but not dominant-negative Rac1, Ras, RalA, Rap1A, or Rap2A) suppresses M3-mediated PLC stimulation. Overexpression/dominant-negative constructs, adenylyl cyclase inhibitor (dd-Ado), clostridial toxin inactivation of Ras-related GTPases, GTP-loading assay for RAP2B, PLC activity assay, Ca2+ measurement in HEK-293 cells The Journal of biological chemistry High 11877431
2004 EGF receptor activates RAP2B via c-Src-dependent tyrosine phosphorylation of RasGRP3 (a Ca2+/diacylglycerol-regulated GEF); activated RAP2B then binds directly to PLC-ε and drives its translocation to the plasma membrane, leading to PLC/Ca2+ signaling. GTP loading of RAP2B by EGF requires intracellular Ca2+ and lipase-active PLC-γ1 (upstream), but not PLC-ε. Dominant-negative RAP2B expression, clostridial toxin treatment, GTP-loading pull-down assay, co-immunoprecipitation of RAP2B with PLC-ε, confocal imaging of PLC-ε translocation, c-Src inhibition, intracellular Ca2+ chelation, in HEK-293 cells Molecular and cellular biology High 15143162
2004 In human platelets, thrombin (via G-protein-coupled receptors) and convulxin (via GPVI/tyrosine kinase pathway) both induce rapid GTP loading of RAP2B. Thrombin-induced RAP2B activation is partially dependent on secreted ADP acting through the Gi-coupled P2Y12 receptor and fully dependent on PI3-kinase activity. Convulxin-induced activation requires PKC and is PI3K-independent. Both are regulated by intracellular Ca2+. cAMP-elevating agents do not activate RAP2B. GTP-loading assay (pull-down with RAP2B-binding domain), pharmacological inhibitors (PI3K inhibitor, PKC inhibitor, ADP scavenger, Ca2+ chelator), P2Y12 antagonist, in primary human platelets Journal of thrombosis and haemostasis High 15613030
2008 RAP2B (but not RAP1B) constitutively associates with lipid rafts in human platelets; this association is mediated by palmitoylation at Cys176 and Cys177 (but not at the CAAX motif). Disruption of lipid raft association by cholesterol depletion impairs agonist-induced RAP2B activation and inhibits platelet aggregation. Lipid raft isolation (detergent-resistant membrane fractionation), [3H]palmitate metabolic labeling, site-directed mutagenesis (C176S, C177S, CAAX deletion) in transfected HEK293T cells and primary platelets, cholesterol depletion, GTP-loading assay, platelet aggregation assay Cellular signalling High 18582561
2013 RAP2B is a direct transcriptional target of p53 that mediates a pro-survival function after DNA damage; p53 binds the RAP2B promoter upon DNA damage and activates its transcription. siRNA knockdown of RAP2B sensitizes cells to DNA damage-induced apoptosis in a p53-dependent manner. Integrative genomic analysis, chromatin immunoprecipitation (p53 binding to RAP2B promoter), siRNA knockdown, apoptosis assays, anchorage-independent growth assay Cell cycle (Georgetown, Tex.) High 23535297
2015 RAP2B promotes breast cancer cell proliferation, migration, and invasion by elevating intracellular calcium levels and promoting ERK1/2 phosphorylation; calcium chelator BAPTA/AM and MEK inhibitor U0126 reverse RAP2B-induced ERK1/2 phosphorylation, placing RAP2B upstream of a Ca2+/ERK1/2 axis. siRNA knockdown and overexpression, CCK-8 proliferation assay, transwell assay, flow cytometry (calcium measurement), Western blot (ERK1/2 phosphorylation), pharmacological inhibitors (BAPTA/AM, U0126) Scientific reports Medium 26201295
2015 RAP2B inhibits cell spreading by disrupting actin dynamics in a CAAX-dependent manner; expression of RAP2B is induced by nocodazole in a p53-dependent manner, and a C180A CAAX mutant of RAP2B does not inhibit cell spreading, demonstrating that membrane targeting is required for cytoskeletal effects. Western blot, immunofluorescence, overexpression and knockdown, site-directed mutagenesis (C180A), nocodazole treatment Journal of cancer research and clinical oncology Medium 25762091
2017 p53 upregulates the RAP2B–PLC-ε–IP3–Ca2+ pathway and thereby inhibits starvation-induced autophagy; p53 induction increases intracellular IP3 and Ca2+ levels and decreases LC3 levels through RAP2B, establishing RAP2B as a mediator of p53-dependent autophagy inhibition. Microarray-based target identification, overexpression/knockdown, measurement of IP3, Ca2+, and LC3 levels by Western blot and biochemical assays Oncotarget Medium 29029384
2016 RAP2B promotes prostate cancer cell migration and invasion via FAK-dependent signaling; elevated RAP2B increases FAK phosphorylation, and FAK-specific inhibitor PF-573228 abolishes RAP2B-induced FAK phosphorylation and the resulting migration/invasion phenotype. siRNA knockdown and overexpression, CCK-8, transwell assay, Western blot (p-FAK), pharmacological inhibitor (PF-573228), xenograft in vivo Medical oncology Medium 27154636
2019 RAP2B knockdown in glioma cells reduces expression levels of NF-κB, MMP-2, and MMP-9, and inhibits cell adhesion, proliferation, migration, and invasion, placing RAP2B upstream of the NF-κB pathway in glioma. siRNA knockdown, Western blot (NF-κB, MMP-2, MMP-9), CCK-8, wound healing, transwell invasion assay Journal of neuro-oncology Medium 30997639
2017 RAP2B promotes renal cell carcinoma angiogenesis in vitro and in vivo via activation of the PI3K/AKT signaling pathway, leading to upregulation of VEGF; this was demonstrated by ELISA measurement of VEGF, HUVEC growth, and tube formation assays with RAP2B knockdown/overexpression. siRNA knockdown and overexpression, Western blot, qPCR, ELISA (VEGF), HUVEC growth assay, endothelial tube formation assay, in vivo tumor model Tumour biology Medium 28691643
2019 Active RAP2B (wild-type) inhibits development of the Coxiella burnetii replicative vacuole (CRV) and impairs both homotypic (phagosome–CRV) and heterotypic (endosome/lysosome–CRV) fusion events; this effect is dependent on RAP2B GTPase activity (inactive ΔAAX mutant has no effect). RAP2B overexpression markedly decreases the v-SNARE Vamp7 levels, suggesting a mechanism involving SNARE downregulation. Transient overexpression of wild-type vs. inactive RAP2B mutant, fluorescence microscopy of vacuole size, fusion assays, Western blot (Vamp7) PloS one Medium 30763357
2024 RAP2B is S-palmitoylated at Cys176 and Cys177 at the C-terminus, which is required for its plasma membrane localization; ABHD17a is identified as the depalmitoylating enzyme for RAP2B, and its PI3K-mediated phosphorylation by EGFR/PI3K signaling regulates ABHD17a activity and thus RAP2B palmitoylation. Mutation of C176/C177 or a blocking peptide targeting these sites causes cytosolic relocation of RAP2B and suppresses CRC cell migration/invasion and metastasis. Site-directed mutagenesis (C176/C177), palmitoylation assays, Co-IP identifying ABHD17a, pharmacological inhibition of PI3K, blocking peptide, xenograft metastasis model Cell death & disease High 39277583
2025 Intestine-specific knockout of RAP2B suppresses CRC initiation and progression in vivo; mechanistically, RAP2B interacts with plectin and enhances plectin expression, which inhibits plectin-mediated F-actin assembly, leading to cytoskeletal remodeling that promotes tumorigenesis and metastasis. Intestine-specific knockout mouse model, co-immunoprecipitation (RAP2B–plectin interaction), Western blot (plectin, F-actin markers), in vivo tumor growth and metastasis assays, human CRC tissue correlation Cell death & disease High 40223002
2009 RAP2B overexpression in Rat1 fibroblasts induces oncogenic transformation foci and activates the NF-κB pathway more than 3-fold as measured by reporter gene assay. Stable transfection in Rat1 cells, colony/focus formation assay, NF-κB reporter gene assay Zhongguo fei ai za zhi (Chinese journal of lung cancer) Medium 20719111
2025 RAP2B overexpression activates the PI3K/AKT signaling pathway and confers resistance to cetuximab in colorectal cancer cells; RAP2B knockdown inhibits PI3K/AKT signaling, reduces cell proliferation, enhances apoptosis, and restores cetuximab sensitivity both in vitro and in vivo. Knockdown and overexpression, Western blot (PI3K/AKT pathway markers), cell proliferation, apoptosis assays, xenograft in vivo Biological procedures online Medium 41094393

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 56 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
2024 Inhibiting S-palmitoylation arrests metastasis by relocating Rap2b from plasma membrane in colorectal cancer. Cell death & disease 12 39277583
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
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 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 7 32596241
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 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

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