Affinage

PREX2

Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein · UniProt Q70Z35

Length
1606 aa
Mass
182.6 kDa
Annotated
2026-06-10
32 papers in source corpus 20 papers cited in narrative 19 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

PREX2 (P-Rex2) is a phosphatidylinositol-(3,4,5)-trisphosphate (PIP3)- and Gβγ-regulated guanine nucleotide exchange factor (GEF) that activates the small GTPase Rac, coupling PI3K and G-protein signaling to Rac-dependent control of cell migration, proliferation, and tissue morphogenesis (PMID:15304343, PMID:15304342, PMID:25829446). PREX2 engages the tumor suppressor PTEN in a mutually inhibitory complex: PTEN's C-terminal PDZ-binding motif binds the second PDZ domain of PREX2, bridging across the protein to block PIP3 hydrolysis, while PTEN reciprocally drives an autoinhibited PREX2 conformation and blocks Gβγ binding; PREX2 inhibition of PTEN requires PTEN C-terminal phosphorylation to release the PREX2 PH domain from its neighboring DH domain (PMID:24367090, PMID:33947796). PIP3 binding through the PREX2 PH domain is critical for GEF activity, and full-length structural analysis shows PREX2 adopts an autoinhibition mechanism divergent from the related P-Rex1, with PIP3-headgroup-independent dynamics (PMID:34958187, PMID:42248461). This complex is held under multiple layers of negative control: PAK kinases phosphorylate PREX2 downstream of Rac1 activation to form a feedback loop that impairs PIP3/Gβγ binding and membrane localization (PMID:26438819); GNMT and the E3 ligase HectH9 drive ubiquitin-proteasomal degradation of PREX2 (PMID:28205209); and CELF2 disrupts the PREX2-PTEN interaction to restore PTEN phosphatase activity (PMID:31241130). Cancer-associated PREX2 truncations and somatic mutations escape PTEN-mediated inhibition or HectH9-mediated degradation, hyperactivating Rac1 and PI3K/AKT signaling to promote invasion, proliferation, and tumorigenesis (PMID:25829446, PMID:33947796, PMID:30796242). Beyond its catalytic role, PREX2 exerts GEF-independent adaptor functions in glucose homeostasis, suppressing hepatic Glut2 surface levels, mitochondrial function, islet insulin secretion, and Gpr21 GPCR trafficking (PMID:40764335). PREX2 is also specifically expressed in cerebellar Purkinje cells, where it is required for normal dendrite morphology and motor coordination (PMID:18334636).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2004 High

    Established the founding biochemical identity of PREX2 as a signal-integrating Rac GEF, answering what enzymatic activity it carries and what regulates it.

    Evidence In vitro GEF assays and in vivo functional assays following cloning from human skeletal muscle and brain libraries, replicated across two labs

    PMID:15304342 PMID:15304343

    Open questions at the time
    • Did not define Rac isoform selectivity in vivo
    • No structural basis for PIP3/Gβγ regulation
  2. 2008 High

    Defined a physiological neuronal role, showing PREX2 is required in cerebellar Purkinje cells for dendrite morphology and motor coordination.

    Evidence Single and double Prex1/Prex2 knockout mice with Purkinje cell morphology imaging and motor behavioral testing

    PMID:18334636

    Open questions at the time
    • Did not establish whether the dendrite phenotype is GEF-dependent
    • Downstream effectors in Purkinje cells not identified
  3. 2012 Medium

    Linked PREX2 to cancer by identifying it as a recurrently mutated, PTEN-interacting gene whose mutants accelerate melanoma formation.

    Evidence Whole-genome sequencing of melanomas and in vivo xenograft tumor formation with mutant PREX2-expressing melanocytes

    PMID:22622578

    Open questions at the time
    • The tumor-acceleration experiment was not reproduced in a later replication study
    • Did not resolve which mutation classes are oncogenic
  4. 2013 High

    Resolved the molecular architecture of PREX2-mediated PTEN inhibition, defining two distinct domain interfaces and a phosphorylation-dependent switch.

    Evidence Domain-mapping and deletion constructs, phosphorylation site analysis, and Prex2 knockout mice with metabolic readouts

    PMID:24367090

    Open questions at the time
    • Did not establish the reciprocal effect of PTEN on PREX2 GEF activity
    • No full-length structure of the complex
  5. 2015 High

    Demonstrated the reciprocal arm of the complex — PTEN inhibits PREX2 GEF activity via its tail independently of phosphatase activity — and showed cancer mutants escape this control.

    Evidence Fluorescent nucleotide exchange GEF assays, MEFs, breast cancer invasion assays, and mutant analysis

    PMID:25829446

    Open questions at the time
    • Structural basis of mutual inhibition not resolved at this stage
    • Did not identify which somatic mutants act by escaping binding versus blocking inhibition
  6. 2015 High

    Identified PAK-mediated phosphorylation as a Rac1-triggered negative feedback loop constraining PREX2 activity and membrane targeting.

    Evidence In vitro GEF assays, mass spectrometry phosphosite mapping, cell fractionation, and insulin stimulation

    PMID:26438819

    Open questions at the time
    • Did not establish phosphatase that reverses PAK sites
    • In vivo relevance of feedback loop not tested
  7. 2017 Medium

    Defined a degradation arm of PREX2 control, showing GNMT and HectH9 drive proteasomal turnover and that their loss activates AKT through PREX2.

    Evidence Co-IP, ubiquitination assays, proteasome inhibitor experiments, siRNA knockdown, and GNMT knockout mice

    PMID:28205209

    Open questions at the time
    • Single lab without reciprocal validation of the GNMT-HectH9-PREX2 axis
    • Ubiquitination site on PREX2 not mapped
  8. 2016 Medium

    Mechanistically connected PREX2 truncations to gain-of-function, showing they activate Rac1 GEF activity and drive PI3K/AKT signaling and proliferation.

    Evidence GEF assays with truncation mutants, AKT phosphorylation readout, and proliferation assays

    PMID:27314100

    Open questions at the time
    • Commentary format with limited methodological detail
    • Did not define which truncation boundaries are required
  9. 2018 High

    Provided the first PREX2 structural data, resolving the PH domain and establishing PIP3 binding as critical for activity but dispensable for membrane localization.

    Evidence X-ray crystallography at 1.9 Å and biochemical PIP3 binding assays

    PMID:34958187

    Open questions at the time
    • Isolated domain only, not full-length context
    • Mechanism of PIP3-independent membrane targeting unresolved
  10. 2019 Medium

    Linked a specific cancer somatic mutation (S1113R) to escape from HectH9 ubiquitination, increasing PREX2 stability and driving migration and AKT activation.

    Evidence Cycloheximide-chase stability assays, ubiquitination assays, migration assays, and AKT phosphorylation analysis

    PMID:30796242

    Open questions at the time
    • Single lab study
    • Structural basis for impaired ubiquitination not defined
  11. 2020 Medium

    Identified CELF2 as a disruptor of the PREX2-PTEN interaction that restores PTEN activity and suppresses proliferation.

    Evidence Co-IP, PTEN phosphatase activity assays, AKT phosphorylation analysis, CELF2 perturbation, and a PDX model

    PMID:31241130

    Open questions at the time
    • Single Co-IP without reciprocal structural mapping
    • Direct versus indirect disruption mechanism unclear
  12. 2021 High

    Resolved the structural logic of the mutual inhibition, defining the PTEN PDZ-motif–PREX2 PDZ2 bridge and showing combined PTEN-inactivating plus PREX2-truncating variants synergistically activate Rac1.

    Evidence Cross-linking mass spectrometry, functional GEF assays, and domain mutant analysis

    PMID:33947796

    Open questions at the time
    • Moderate structural resolution, no atomic model of full complex
    • Did not test combinatorial variants in vivo
  13. 2022 Medium

    Extended neuronal function beyond cerebellum, showing PREX2 controls AMPA receptor trafficking and dendritic spine morphology via Rac1/pGluR1 in dorsal horn neurons during bone cancer pain.

    Evidence Intrathecal RNAi, Western blot of p-Rac1/p-GluR1, spine imaging, and patch-clamp AMPAR recordings

    PMID:35083941

    Open questions at the time
    • Single lab without genetic knockout confirmation
    • Direct GEF-substrate link to GluR1 trafficking not established
  14. 2024 Medium

    Connected PREX2 to therapy resistance, showing it facilitates DNA repair via DNA-PKcs and suppresses radiation-induced immunogenic cell death through cGAS/STING/IFN inhibition.

    Evidence RNA-seq, Western blot, colony formation, comet assay, xenografts, and the small-molecule inhibitor PREX-in1

    PMID:38609982

    Open questions at the time
    • Mechanism linking GEF activity to DNA-PKcs upregulation unresolved
    • Single lab
  15. 2025 High

    Dissected GEF-independent adaptor functions, showing PREX2 suppresses glucose uptake, Glut2 surface levels, mitochondrial function, insulin secretion, and Gpr21 trafficking independently of catalysis.

    Evidence Prex2 knockout and catalytically-inactive Prex2GD knock-in mice with glucose uptake, Glut2 surface, mitochondrial, insulin secretion, and GPCR trafficking assays

    PMID:40764335

    Open questions at the time
    • Molecular adaptor mechanism for Gpr21/Glut2 trafficking not defined
    • Binding partners mediating adaptor function unidentified
  16. 2025 Medium

    Established a druggable PREX2/RAC1/PI3Kβ axis, showing PREX2 loss sensitizes BRAF-mutant melanoma to MAPK inhibitors and PI3Kβ inhibition phenocopies PREX2 deficiency.

    Evidence PREX2-deletion mouse models, patient-derived BRAFV600E melanoma lines, pharmacologic PI3Kβ inhibition, and MAPK inhibitor sensitivity assays

    PMID:39636745

    Open questions at the time
    • Single lab
    • Clinical applicability of the axis untested
  17. 2025 Medium

    Identified AHCYL1 as an activating interactor that relieves PREX2-PTEN mutual inhibition to amplify Rac1 activation and tumor promotion in NSCLC.

    Evidence Pull-down with LC-MS/MS, in vitro GEF assays, active Rac1 pull-down, Western blot, and a CDX mouse model

    PMID:40365293

    Open questions at the time
    • Single lab without reciprocal interaction mapping
    • Structural basis for relief of inhibition unknown
  18. 2026 High

    Resolved full-length PREX2 architecture, revealing a repositioned N-terminal module and IP4-independent dynamics indicating an autoinhibition mechanism divergent from P-Rex1.

    Evidence Cryo-EM, HDX-MS, SEC-SAXS, and in vitro GEF assays (peer-reviewed, with a parallel preprint version)

    PMID:41542420 PMID:42248461

    Open questions at the time
    • Moderate cryo-EM resolution limits side-chain detail
    • Conformational transition to the active GEF state not captured

Open questions

Synthesis pass · forward-looking unresolved questions
  • The molecular identity of the adaptor-mode binding partners that mediate GEF-independent control of Glut2 and Gpr21 trafficking, and how membrane targeting occurs without PIP3 binding, remain open.
  • No partner identified for the adaptor function
  • Mechanism of PIP3-independent membrane localization unresolved
  • Active-state structural transition uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0008289 lipid binding 1 GO:0060089 molecular transducer activity 1 GO:0060090 molecular adaptor activity 1
Localization
GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1643685 Disease 2
Partners
AHCYL1CELF2GNMTHECTH9PAKPTENRAC1
Complex memberships
PTEN:P-Rex2 complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 PREX2 (P-Rex2) is a guanine-nucleotide exchange factor (GEF) that activates the small GTPase Rac and is regulated by phosphatidylinositol (3,4,5)-trisphosphate (PIP3) and Gβγ subunits of heterotrimeric G proteins in vitro and in vivo. In vitro GEF assay, in vivo functional assays; cloning from human skeletal muscle and brain libraries FEBS letters High 15304342 15304343
2013 P-REX2 inhibits PTEN through two interfaces: the PH domain of P-REX2 inhibits PTEN by interacting with its catalytic region, while the inositol polyphosphate 4-phosphatase (IP4P) domain of P-REX2 provides high-affinity binding to the PDZ-binding domain of PTEN. P-REX2 inhibition of PTEN requires C-terminal phosphorylation of PTEN to release the P-REX2 PH domain from its neighboring DH domain. Domain-mapping biochemical assays, deletion constructs, phosphorylation site analysis; Prex2 knockout mice showing increased Pten activity and decreased insulin signaling Proceedings of the National Academy of Sciences of the United States of America High 24367090
2015 PTEN inhibits PREX2 GEF activity toward RAC1, thereby suppressing cell migration and invasion. This inhibition requires the tail domain of PTEN but not its lipid phosphatase activity. Cancer-derived somatic PREX2 mutants are resistant to PTEN-mediated inhibition of invasion and either escape PTEN binding or are not blocked in their GEF activity by PTEN. Fluorescent nucleotide exchange assays (in vitro GEF assay), mouse embryonic fibroblasts, breast cancer cell line invasion assays, domain deletion/mutant analysis Science signaling High 25829446
2015 PAK kinases phosphorylate PREX2 following Rac1 activation, creating a negative feedback loop. PAK-mediated phosphorylation of PREX2 reduces its GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ, and also prevents PREX2 from localizing to the cellular membrane. In vitro GEF assays, mass spectrometry phosphorylation mapping, cell fractionation, insulin stimulation experiments The Journal of biological chemistry High 26438819
2008 P-Rex2 is specifically expressed in Purkinje neurons of the cerebellum and is required for Purkinje cell dendrite morphology and motor coordination. P-Rex2 knockout mice show thinned main dendrites in Purkinje cells, progressive motor coordination defects, and double P-Rex1/P-Rex2 knockout mice are ataxic. P-Rex2 knockout mouse generation and analysis, Purkinje cell morphology imaging, behavioral motor coordination tests Proceedings of the National Academy of Sciences of the United States of America High 18334636
2021 The PTEN:P-Rex2 complex is assembled via PDZ-interacting motif in the PTEN C-terminal tail binding to the second PDZ domain of P-Rex2, bridging PTEN across the P-Rex2 surface to block PI(3,4,5)P3 hydrolysis. Conversely, PTEN allosterically promotes an autoinhibited conformation of P-Rex2 and blocks its binding to Gβγ. Cancer-associated PTEN-deactivating mutations combined with P-Rex2 truncations drive Rac1 activation to a greater extent than either single variant alone. Cross-linking mass spectrometry, functional GEF assays, domain mutant analysis Science signaling High 33947796
2017 GNMT interacts with PREX2 and promotes its degradation through an E3 ligase HectH9-mediated proteasomal ubiquitination pathway. Depletion of GNMT or HectH9 results in AKT activation in a PREX2-dependent manner. Co-immunoprecipitation, ubiquitination assay, proteasome inhibitor experiments, siRNA knockdown, GNMT knockout mice International journal of cancer Medium 28205209
2018 The crystal structure of the P-Rex2 PH domain at 1.9 Å resolution reveals conformational differences in loop regions compared to P-Rex1. Biochemical studies show the P-Rex2 PH domain binds PIP3 similarly to P-Rex1; binding is critical for P-Rex2 activity but not for membrane localization. X-ray crystallography (1.9 Å), biochemical PIP3 binding assays Journal of structural biology: X High 34958187
2026 Cryo-EM structure of full-length P-Rex2 reveals that, while overall similar to P-Rex1, there is a substantial repositioning of the N-terminal module relative to the C-terminal core, potentially precluding intramolecular autoinhibitory interactions seen in P-Rex1. HDX-MS shows P-Rex2 dynamics are unaffected by IP4 (PIP3 headgroup), unlike P-Rex1, suggesting a different autoinhibition mechanism. Cryo-EM (moderate resolution), hydrogen-deuterium exchange mass spectrometry (HDX-MS), SEC-SAXS, biochemical GEF assays The Journal of biological chemistry High 42248461
2012 Ectopic expression of mutant PREX2 accelerates tumor formation of immortalized human melanocytes in vivo, establishing PREX2 as a functionally relevant mutated gene in melanoma. PREX2 was identified as a PTEN-interacting protein and negative regulator of PTEN. Whole-genome sequencing of 25 melanomas; in vivo xenograft tumor formation assay with mutant PREX2-expressing melanocytes Nature Medium 22622578
2016 Truncating PREX2 mutations activate its RAC1 guanine nucleotide exchanger activity, leading to increased PI3K/AKT signaling and enhanced cell proliferation. GEF activity assays with truncation mutants, AKT phosphorylation readout, cell proliferation assays Molecular & cellular oncology Medium 27314100
2019 The PREX2 somatic mutation S1113R (identified in HCC) impairs HectH9-mediated ubiquitination of PREX2, resulting in extended protein half-life and enhanced protein stability, and promotes cell migration and AKT pathway activation. Protein stability/half-life assays (cycloheximide chase), ubiquitination assay, cell migration assay, AKT phosphorylation analysis Scientific reports Medium 30796242
2020 CELF2 interacts with PREX2 and reduces the association of PREX2 with PTEN, thereby upregulating PTEN phosphatase activity and suppressing AKT phosphorylation and cell proliferation. Co-immunoprecipitation (CELF2-PREX2 interaction), PTEN phosphatase activity assay, AKT phosphorylation analysis, CELF2 overexpression/knockdown, PDX tumor model Carcinogenesis Medium 31241130
2022 P-Rex2 regulates GluR1-containing AMPA receptor trafficking and dendritic spine morphology via Rac1/pGluR1 pathway in dorsal horn neurons, contributing to bone cancer pain. P-Rex2 knockdown reduced spinal p-Rac1, p-GluR1, spine number, and reversed AMPAR-induced current in dorsal horn neurons. Intrathecal RNAi lentivirus injection, Western blot for p-Rac1/p-GluR1, spine density imaging, whole-cell patch clamp recording of AMPAR currents Molecular pain Medium 35083941
2025 AHCYL1 is a novel PREX2-interacting protein that enhances PREX2 GEF activity by alleviating the mutual inhibition between PREX2 and PTEN, thereby intensifying PREX2-driven Rac1 activation and tumor-promoting effects in NSCLC. Pull-down assay with LC-MS/MS (identification of AHCYL1), in vitro GEF assay, active Rac1 pull-down assay, Western blotting, CDX mouse model Theranostics Medium 40365293
2025 P-Rex2 suppresses glucose uptake into liver and skeletal muscle independently of its catalytic (GEF) activity, as shown using catalytically-inactive Prex2GD knock-in mice. In hepatocytes, P-Rex2 suppresses Glut2 cell-surface levels, mitochondrial membrane potential, and ATP production. P-Rex2 also suppresses insulin secretion by pancreatic islets. The orphan GPCR Gpr21 was identified as a P-Rex2 target, with P-Rex2 proposed to limit hepatic glucose clearance by controlling Gpr21 trafficking. Prex2 knockout and catalytically-inactive Prex2GD knock-in mice, glucose uptake assays, Glut2 surface localization assay, mitochondrial function assay, insulin secretion assay, GPCR trafficking studies Scientific reports High 40764335
2024 PREX2 promotes radiation resistance in colorectal cancer by facilitating DNA repair through upregulation of DNA-PKcs and suppressing radiation-induced immunogenic cell death and CD8+ T cell infiltration via inhibition of the cGAS/STING/IFN signaling pathway. RNA-seq, Western blotting, colony formation assay, apoptosis assay, comet assay, xenograft tumor models, small-molecule PREX2 inhibitor (PREX-in1) BMC medicine Medium 38609982
2025 Genetic loss of PREX2 in BRAF-mutant melanoma confers sensitivity to MAPK pathway inhibitors, and pharmacologic targeting of PI3Kβ (downstream of PREX2/RAC1) phenocopies PREX2 deficiency, establishing a druggable PREX2/RAC1/PI3Kβ signaling axis. Genetically engineered mouse models (PREX2 deletion), patient-derived BRAFV600E melanoma cell lines, pharmacologic PI3Kβ inhibition, MAPK inhibitor sensitivity assays Cancer research Medium 39636745
2026 Cryo-EM structure of full-length P-Rex2 (preprint version) shows substantial repositioning of the N-terminal module relative to C-terminal core compared to P-Rex1; HDX-MS shows P-Rex2 is unaffected by IP4 unlike P-Rex1; biochemical assays indicate P-Rex2 may be more tightly regulated by autoinhibition via a mechanism divergent from P-Rex1. Cryo-EM, HDX-MS, SEC-SAXS, in vitro GEF assays bioRxivpreprint Medium 41542420

Source papers

Stage 0 corpus · 32 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Melanoma genome sequencing reveals frequent PREX2 mutations. Nature 590 22622578
2004 P-Rex2, a new guanine-nucleotide exchange factor for Rac. FEBS letters 89 15304343
2004 P-REX2, a novel PI-3-kinase sensitive Rac exchange factor. FEBS letters 83 15304342
2015 PTEN inhibits PREX2-catalyzed activation of RAC1 to restrain tumor cell invasion. Science signaling 63 25829446
2008 P-Rex2 regulates Purkinje cell dendrite morphology and motor coordination. Proceedings of the National Academy of Sciences of the United States of America 59 18334636
2013 Regulation of PTEN inhibition by the pleckstrin homology domain of P-REX2 during insulin signaling and glucose homeostasis. Proceedings of the National Academy of Sciences of the United States of America 58 24367090
2020 CELF2 suppresses non-small cell lung carcinoma growth by inhibiting the PREX2-PTEN interaction. Carcinogenesis 44 31241130
2017 P-Rex1 and P-Rex2 RacGEFs and cancer. Biochemical Society transactions 39 28710285
2017 Characterization of the GNMT-HectH9-PREX2 tripartite relationship in the pathogenesis of hepatocellular carcinoma. International journal of cancer 28 28205209
2014 The effect of CXCL9 on the invasion ability of hepatocellular carcinoma through up-regulation of PREX2. Journal of molecular histology 27 25151370
2019 Involvement of TLR4/ CXCL9/ PREX-2 pathway in the development of hepatocellular carcinoma (HCC) and the promising role of early administration of lactobacillus plantarum in Wistar rats. Tissue & cell 22 31582017
2019 Somatic mutations of PREX2 gene in patients with hepatocellular carcinoma. Scientific reports 21 30796242
2017 Replication Study: Melanoma genome sequencing reveals frequent PREX2 mutations. eLife 20 28100394
2015 p21-activated Kinases (PAKs) Mediate the Phosphorylation of PREX2 Protein to Initiate Feedback Inhibition of Rac1 GTPase. The Journal of biological chemistry 20 26438819
2024 PREX2 contributes to radiation resistance by inhibiting radiotherapy-induced tumor immunogenicity via cGAS/STING/IFNs pathway in colorectal cancer. BMC medicine 16 38609982
2016 Upregulation of PREX2 promotes the proliferation and migration of hepatocellular carcinoma cells via PTEN-AKT signaling. Oncology letters 16 26998152
2021 Structural analysis of the PTEN:P-Rex2 signaling complex reveals how cancer-associated mutations coordinate to hyperactivate Rac1. Science signaling 13 33947796
2016 PREX2 promotes the proliferation, invasion and migration of pancreatic cancer cells by modulating the PI3K signaling pathway. Oncology letters 10 27446408
2025 Targeting the PREX2/RAC1/PI3Kβ Signaling Axis Confers Sensitivity to Clinically Relevant Therapeutic Approaches in Melanoma. Cancer research 7 39636745
2018 Structural and biochemical characterization of the pleckstrin homology domain of the RhoGEF P-Rex2 and its regulation by PIP3. Journal of structural biology: X 5 34958187
2016 Mechanistic insights into the role of truncating PREX2 mutations in melanoma. Molecular & cellular oncology 5 27314100
2021 PREX2 gene's expression in gastric antral epithelial cells of patients with H. pylori infection. Arquivos de gastroenterologia 4 34705970
2025 P-Rex2 suppresses glucose uptake into liver and skeletal muscle through different adaptor functions. Scientific reports 3 40764335
2022 P-Rex2 mediation of synaptic plasticity contributes to bone cancer pain. Molecular pain 3 35083941
2014 Registered report: Melanoma genome sequencing reveals frequent PREX2 mutations. eLife 3 25490935
2013 P-Rex2, a Rac-guanine nucleotide exchange factor, is expressed selectively in ribbon synaptic terminals of the mouse retina. BMC neuroscience 3 23844743
2026 P-Rex2 exhibits unique structural features and regulatory mechanisms distinct from the closely related RhoGEF P-Rex1. bioRxiv : the preprint server for biology 2 41542420
2025 AHCYL1 mediates the tumor-promoting effect of PREX2 in non-small cell lung carcinoma. Theranostics 1 40365293
2025 Unraveling the role of PREX2 mutations as a biomarker for immunotherapy response in colorectal cancer. Cancer biomarkers : section A of Disease markers 1 40971540
2022 Sustainable and cost-effective ternary electrolyte Et3NHCl-AlCl3-Mg(DEP)2 for high-performance rechargeable magnesium batteries. Physical chemistry chemical physics : PCCP 1 34988572
2026 The Rho guanine-nucleotide exchange factor P-Rex2 exhibits structural and regulatory features distinct from the related RhoGEF P-Rex1. The Journal of biological chemistry 0 42248461
2021 PREX2 promotes the proliferation, invasion and migration of pancreatic cancer cells by modulating the PI3K signaling pathway. Oncology letters 0 34386078

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