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Showing RACGAP1 — MGCRACGAP is a alias.

RACGAP1

Rac GTPase-activating protein 1 · UniProt Q9H0H5

Length
632 aa
Mass
71.0 kDa
Annotated
2026-06-10
93 papers in source corpus 39 papers cited in narrative 40 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RACGAP1 (MgcRacGAP) is a multifunctional RhoGAP that governs the spatial control of Rho-family GTPase activity during cytokinesis and, in distinct contexts, acts as a nuclear transport chaperone and a stabilizer of oncogenic transcription factors (PMID:9497316, PMID:16129829, PMID:17178910). Its GAP domain potently stimulates Rac1 and Cdc42 GTPase activity while being nearly inactive on RhoA, and membrane-reconstituted biochemistry and crystallography establish marked Rac1 selectivity that is potentiated by phosphatidylserine and PIP2 acting through its C1 and GAP domains (PMID:9497316, PMID:41676911, PMID:23665020). During mitosis RACGAP1 localizes to the spindle and condenses at the midbody, binding tubulins through its N-terminal myosin-like domain; both this localization and GAP activity are required for cytokinesis, and its loss produces binucleation and pre-implantation lethality in mice (PMID:11085985, PMID:11287179). It dimerizes with the MKLP1/ZEN-4 kinesin to form the heterotetrameric centralspindlin complex that bundles microtubules, and an SxIP motif tethers it to EB1/EB3 on microtubule plus ends to position it at the contractile ring (PMID:17942600, PMID:28389580). RACGAP1 controls cleavage-furrow RhoA activation through a non-canonical mechanism: Plk1 phosphorylation of Ser157/Ser164 together with centralspindlin assembly recruits the RhoGEF ECT2, and CYK-4/RACGAP1 GAP activity at the plasma membrane promotes RhoA-GTP hydrolysis to activate ECT2 rather than inactivate RhoA, driving contractile-ring assembly and myosin light-chain phosphorylation (PMID:16129829, PMID:25486482, PMID:26252513). Aurora B phosphorylation at Ser387 modulates substrate preference by selectively weakening Cdc42 engagement, as resolved by crystal structures of the GAP domain bound to CDC42 and RHOA transition-state mimics (PMID:12689593, PMID:39522789). Independent of cytokinesis, RACGAP1 with GTP-Rac1 and importins drives nuclear import of phospho-STAT3/STAT5 (PMID:17178910, PMID:19158271), competes with ARNT for the HIF-1α PAS-B domain to block HIF-1 transcription (PMID:23458834), and in cancer is recruited via Akt-dependent phosphorylation to IQGAP1 complexes at pseudopod tips to locally switch Rac1 to RhoA and promote invasion (PMID:24019536, PMID:23843620). It is degraded by APC(CDH1) in late M/G1 (PMID:23696789).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1998 High

    Established the founding biochemical identity of RACGAP1 as a RhoGAP, defining which GTPases it acts on in vitro.

    Evidence In vitro GAP activity assays with recombinant GAP domain and domain analysis

    PMID:9497316

    Open questions at the time
    • In vitro substrate preference (Rac1/Cdc42 over RhoA) did not predict the in-cell RhoA-directed function
    • No structural basis for catalysis at this stage
  2. 2000 High

    Showed RACGAP1 is a cytokinesis factor by linking its dynamic mitotic localization and GAP activity to division, answering whether it had a cell-cycle role.

    Evidence Immunofluorescence, tubulin co-IP, and deletion/GAP-dead mutants in HeLa cells; gain-of-function in HL-60 cells

    PMID:10979956 PMID:11085985

    Open questions at the time
    • Mechanism linking localization to RhoA regulation not yet defined
    • GAP-independent differentiation function mechanistically unexplained
  3. 2001 High

    Demonstrated RACGAP1 is non-redundantly essential for cytokinesis in vivo, ruling out compensation by paralogs.

    Evidence Gene-trap mouse knockout with binucleated blastomere phenotype

    PMID:11287179

    Open questions at the time
    • Did not separate cytokinetic from other potential developmental roles
    • No molecular mechanism for the failure
  4. 2003 High

    Identified Aurora B phosphorylation of Ser387 as a regulatory switch and placed GAP activity upstream of RhoA, addressing how RACGAP1 directs cortical activity during cytokinesis.

    Evidence In vitro kinase assays, S387A/S387D mutants, colocalization, and GAP-dead R386A epistasis with RhoA mutants

    PMID:12689593 PMID:14729465

    Open questions at the time
    • Whether Ser387 phosphorylation truly switches substrate to RhoA was later contested
    • Connection to the GEF that activates RhoA not yet established
  5. 2003 Medium

    Identified tissue-specific GTPase and partner contexts, including Rnd2 in male germ cells, expanding the partner repertoire beyond canonical mitotic GTPases.

    Evidence GST pull-down, co-IP, and colocalization in spermatocytes/spermatids

    PMID:12590651

    Open questions at the time
    • Functional significance of the Rnd2 interaction not tested by loss-of-function
    • Single lab
  6. 2004 High

    Showed PRC1 binding inhibits RACGAP1 GAP activity and that Aurora B phosphorylation relieves this inhibition, defining a temporal control mechanism across mitosis.

    Evidence Yeast two-hybrid, co-IP, in vitro GAP assays, and phosphorylation assays with domain mapping

    PMID:14744859

    Open questions at the time
    • In-cell quantitative contribution of PRC1 inhibition not established
    • Single lab
  7. 2005 High

    Connected RACGAP1 to ECT2 recruitment and contractile-ring/myosin activation, answering how it engages the RhoA-activating machinery at the furrow.

    Evidence RNAi epistasis, co-IP, contractile-ring assembly assays, and Cdk1-inhibition pathway experiments; Cdc42 regulation in metaphase

    PMID:15642749 PMID:16118207 PMID:16129829

    Open questions at the time
    • How GAP activity and GEF recruitment are reconciled mechanistically not yet resolved
    • Phospho-dependence of ECT2 binding not defined
  8. 2006 High

    Revealed a GAP-independent, scaffold-based role: RACGAP1 acts as an NLS-containing nuclear chaperone importing activated STATs, broadening its function beyond cytokinesis.

    Evidence Reconstituted permeabilized-cell nuclear import with purified Rac1, importins, and p-STAT5A; B-cell rescue with GAP-dead mutant

    PMID:16959247 PMID:17178910

    Open questions at the time
    • How RACGAP1 partitions between cytokinetic and nuclear-transport pools unclear
    • Physiological STAT signaling outputs not mapped
  9. 2007 High

    Defined centralspindlin architecture and showed the assembled complex, not isolated subunits, bundles microtubules; identified HIF-1α inhibition as a new RACGAP1 function.

    Evidence Biochemical reconstitution, microtubule bundling assay, suppressor genetics; HIF-1 reporter and binding assays

    PMID:17942600 PMID:17982282

    Open questions at the time
    • Mechanism of HIF-1α inhibition not yet resolved at this stage
    • Stoichiometry of centralspindlin on microtubules in cells not addressed
  10. 2008 Medium

    Showed PP2A-B56ε dephosphorylation is required for RACGAP1–ECT2 interaction, adding phosphatase counter-regulation to the kinase inputs.

    Evidence Co-IP, in vitro phosphorylation, and PP2A inhibition with identification of B56ε

    PMID:18201571

    Open questions at the time
    • Site-specific dephosphorylation events not mapped
    • Single lab
  11. 2013 High

    Mechanistically dissected the HIF-1α block (ARNT competition at PAS-B), nuclear-chaperone STAT phosphorylation requirement, APC(CDH1) degradation, the GAP-domain crystal structure, and integrin/IQGAP1-based invasion roles, building a multidomain functional map.

    Evidence Pull-downs and competition assays, NLS/STAT mutants, degron mapping, X-ray crystallography of GAP domain, and integrin adhesion proteomics with invasion assays

    PMID:19158271 PMID:23458834 PMID:23665020 PMID:23696789 PMID:23843620 PMID:24019536 PMID:24807907

    Open questions at the time
    • How phosphorylation routes RACGAP1 to invasion versus cytokinesis complexes not fully defined
    • Several findings rest on single-lab evidence
  12. 2014 Medium

    Resolved the Plk1-driven ECT2 recruitment code (Ser157/Ser164 plus centralspindlin assembly) and the Trio-Rac1 antagonism, refining how RACGAP1 sets the spatial GTPase balance at the furrow.

    Evidence Phospho-site mapping with BRCT-binding assays and MKLP1 depletion; RNAi epistasis with GEF-dead Trio mutants; endothelial RhoA/FAK signaling assays; germ-cell conditional knockout

    PMID:24355749 PMID:25355950 PMID:25475728 PMID:25486482

    Open questions at the time
    • Quantitative integration of opposing Trio and RACGAP1 activities not modeled
    • Endothelial RhoA role uses single-lab functional assays
  13. 2015 High

    Established the non-canonical mechanism by which CYK-4/RACGAP1 GAP activity activates RhoA via ECT2 at the membrane, and challenged the simple Ser387 substrate-switch model in vertebrate epithelia.

    Evidence C. elegans genetics with in vitro CYK-4/ECT-2 domain interaction and suppressor mutations; Xenopus FRET biosensors with GAP-dead and S386A/D mutants

    PMID:25947135 PMID:26252513

    Open questions at the time
    • Reconciliation of in vitro Rac1 preference with in-cell RhoA-directed activation incomplete
    • Role of Ser386/387 phosphorylation context-dependent and unresolved
  14. 2016 Medium

    Showed RACGAP1 functions dose-dependently across sequential cytokinesis steps, indicating distinct thresholds for abscission, ingression, and furrow initiation.

    Evidence Graded zebrafish loss-of-function (ogre mutant) with live imaging

    PMID:27339293

    Open questions at the time
    • Molecular basis of step-specific thresholds not defined
    • Single lab
  15. 2017 Medium

    Demonstrated the SxIP motif tethers centralspindlin to EB1/EB3 on growing microtubule plus ends to spatially position RACGAP1 and RhoA at the contractile ring.

    Evidence SxIP mutagenesis with EB3 live imaging and RhoA localization in Xenopus embryos

    PMID:28389580

    Open questions at the time
    • Relative contribution of plus-end tracking versus central-spindle localization not quantified
    • Single lab
  16. 2019 Medium

    Connected the nuclear-chaperone activity to a cancer signaling circuit, defining a RACGAP1→STAT3→DNMT3B→ESR1 feedback loop in bladder cancer.

    Evidence Overexpression/knockdown, STAT3 phosphorylation and nuclear translocation assays, and ChIP/methylation analysis

    PMID:30511377

    Open questions at the time
    • Directness of RACGAP1-driven STAT3 phosphorylation not biochemically reconstituted
    • Single lab
  17. 2021 Low

    Linked RACGAP1 to mitochondrial fission through ECT2 recruitment and the ERK-DRP1 pathway, proposing an organelle-dynamics role beyond cytokinesis.

    Evidence Co-IP, mitochondrial morphology, mitophagy and DRP1 phosphorylation assays with overexpression/knockdown

    PMID:33485843

    Open questions at the time
    • Mechanistic claims rely on indirect readouts without in vitro reconstitution
    • Single lab, not independently confirmed
  18. 2024 High

    Provided the structural basis for the Ser387 substrate-preference shift and refined the membrane-dependent Rac1 selectivity, resolving the longstanding RhoA-versus-Rac1 substrate question biochemically.

    Evidence Crystal structures of GAP domain with CDC42 and RHOA transition-state mimics, S387D/A activity assays; membrane reconstitution with crystallography and Rac1 specificity mutagenesis; AR-driven feedback and EZH2 stabilization assays

    PMID:37196108 PMID:38898473 PMID:39522789 PMID:41676911

    Open questions at the time
    • How biochemical Rac1 selectivity is overridden to drive RhoA activation in cells still not fully mechanistically unified
    • Cancer transcription-factor stabilization roles rest on single-lab evidence
  19. 2025 Medium

    Identified MARCH5-mediated ubiquitination as a degradation route controlling RACGAP1 levels and DRP1-driven mitochondrial fission, extending the regulation of RACGAP1 stability beyond APC(CDH1).

    Evidence Co-IP/MS, ubiquitination assay, and in vivo rescue in an aortic valve calcification mouse model

    PMID:39880131

    Open questions at the time
    • Direct ubiquitination sites not mapped
    • Relationship to APC(CDH1)-dependent degradation not integrated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How RACGAP1 is partitioned among its cytokinetic, nuclear-transport, transcription-factor-stabilizing, and mitochondrial roles by upstream phosphorylation and localization cues remains unresolved.
  • No unified model reconciling membrane Rac1 selectivity with in-cell RhoA activation
  • Physiological versus cancer-specific role switching not defined
  • Lipid-species interactions during division uncharacterized functionally

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 6 GO:0008092 cytoskeletal protein binding 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0060090 molecular adaptor activity 2 GO:0008289 lipid binding 1
Localization
GO:0005634 nucleus 3 GO:0005856 cytoskeleton 2 GO:0005886 plasma membrane 2
Pathway
R-HSA-1640170 Cell Cycle 4 R-HSA-162582 Signal Transduction 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-9609507 Protein localization 2
Partners
AREB1ECT2EZH2HIF1AIQGAP1MKLP1PRC1
Complex memberships
IQGAP1/filamin-A complex at active β1 integrincentralspindlin (with MKLP1/ZEN-4)

Evidence

Reading pass · 40 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 MgcRacGAP (RACGAP1) was identified as a GTPase-activating protein (GAP) whose GAP domain strongly stimulates Rac1 and Cdc42 GTPase activity in vitro but is almost inactive on RhoA. The protein contains an N-terminal cysteine-rich zinc finger-like motif characteristic of the Chimaerin family of RhoGAPs. In vitro GAP activity assay with recombinant protein; two-hybrid cloning; domain analysis The Journal of biological chemistry High 9497316
2000 MgcRacGAP localizes to the nucleus in interphase, accumulates on the mitotic spindle in metaphase, and condenses at the midbody during cytokinesis. It binds alpha-, beta-, and gamma-tubulins through its N-terminal myosin-like domain. An N-terminal deletion mutant that loses mitotic spindle/midbody localization causes multinucleation, and a GAP-inactive mutant also causes cytokinesis failure, indicating both localization and GAP activity are required. Anti-MgcRacGAP antibody immunofluorescence; co-immunoprecipitation with tubulins; overexpression of deletion and GAP-inactive mutants in HeLa cells The Journal of biological chemistry High 11085985
2000 MgcRacGAP overexpression alone induces growth suppression and macrophage differentiation in HL-60 leukemic cells. The GAP activity is dispensable for this function, but the myosin-like domain and the cysteine-rich domain are required, indicating a GAP-independent mechanism for regulating hematopoietic cell growth and differentiation. Retroviral overexpression; GAP-inactive mutant and deletion mutant analysis; flow cytometry for CD14 expression Blood Medium 10979956
2001 Homozygous loss-of-function of mgcRacGAP in mice causes pre-implantation lethality with binucleated blastomeres, demonstrating that MgcRacGAP is essential for cytokinesis during early embryogenesis and is functionally non-redundant. Gene trap mouse model; embryo phenotypic analysis; immunostaining Mechanisms of development High 11287179
2003 Aurora B phosphorylates MgcRacGAP on serine residues (including Ser387) and this modification converts its latent GAP activity toward RhoA in vitro. A kinase-defective Aurora B mutant inhibits Ser387 phosphorylation but not midbody localization. Overexpression of phosphorylation-deficient MgcRacGAP-S387A arrests cytokinesis and induces polyploidy, whereas S387D (phospho-mimic) does not. MgcRacGAP colocalizes with Aurora B and RhoA (but not Rac1/Cdc42) at the midbody. In vitro kinase assay; phospho-specific analysis; overexpression of S387A and S387D mutants; immunofluorescence colocalization Developmental cell High 12689593
2003 Rho family GTPase Rnd2 forms a stable complex with MgcRacGAP in male germ cells (spermatocytes/spermatids), demonstrated by GST pull-down and co-immunoprecipitation. They co-localize at the Golgi-derived pro-acrosomal vesicle and at the midzone of meiotic cells, identifying Rnd2 as a probable physiological partner of MgcRacGAP in male germ cells. GST pull-down; co-immunoprecipitation; immunofluorescence colocalization The Biochemical journal Medium 12590651
2004 PRC1 (protein-regulating cytokinesis 1) binds the C-terminal GAP-conserved domain of MgcRacGAP and inhibits its GAP activity toward Cdc42 during metaphase. PRC1 binding depends on the basic region (125-285 aa) of MgcRacGAP. Aurora B phosphorylation of the basic region prevents PRC1-mediated inhibition of GAP activity, thereby switching MgcRacGAP activity during mitotic progression. Yeast two-hybrid; co-immunoprecipitation; in vitro GAP activity assay; phosphorylation assay The Journal of biological chemistry High 14744859
2004 Expression of a GAP-deficient MgcRacGAP mutant (R386A) induces abnormal cortical blebbing during cytokinesis via RhoA. Dominant-negative RhoA (but not dominant-negative Rac1 or Cdc42) suppresses this phenotype, and constitutively active RhoA phenocopies it, placing MgcRacGAP's GAP activity upstream of RhoA in cortical activity regulation during cytokinesis. Expression of GAP-dead mutant R386A; dominant-negative and constitutively active RhoA/Rac1/Cdc42 epistasis; live cell imaging Experimental cell research Medium 14729465
2005 MgcRacGAP is required for assembly of anillin and myosin into the contractile ring and for RhoA-mediated phosphorylation of myosin regulatory light chain. MgcRacGAP associates with ECT2 (a RhoA GEF) during cytokinesis, and localization of ECT2 to the central spindle and contractile ring depends on MgcRacGAP. Knockdown of ECT2 phenocopies MgcRacGAP knockdown. RNAi knockdown; immunofluorescence; co-immunoprecipitation; contractile ring assembly assays Proceedings of the National Academy of Sciences of the United States of America High 16129829
2005 Ect2 and MgcRacGAP regulate the activation of Cdc42 in metaphase. GTP-Cdc42 levels elevate in metaphase and are suppressed by dominant-negative Ect2 or MgcRacGAP mutants, or by Ect2 RNAi. Depletion of Ect2 impairs microtubule attachment to kinetochores, suggesting Ect2-MgcRacGAP regulate Cdc42 for correct spindle assembly. Pull-down assay for GTP-Cdc42; dominant-negative overexpression; RNAi; immunofluorescence for kinetochore attachment The Journal of cell biology Medium 15642749
2005 Inhibition of Cdk1 is sufficient to initiate cytokinesis (including contractile ring formation and blebbing) in an ECT2- and MgcRacGAP-dependent manner. RNAi depletion of ECT2 or MgcRacGAP abolishes Cdk1-inhibition-induced furrow formation, and dominant-negative or depleted RhoA also blocks the phenotype, placing Cdk1→ECT2/MgcRacGAP→RhoA in a cytokinesis initiation pathway. Cdk1 inhibitor treatment; RNAi knockdown of ECT2, MgcRacGAP, RhoA; dominant-negative RhoA expression; live cell imaging The Journal of biological chemistry Medium 16118207
2006 MgcRacGAP and GTP-bound Rac1 bind directly to phosphorylated STAT5A and are required for its nuclear translocation. In permeabilized cell assays, nuclear import of purified p-STAT5A requires GTP-Rac1, MgcRacGAP, importin alpha, and importin beta. STAT3 uses the same transport machinery. MgcRacGAP functions as an NLS-containing nuclear transport chaperone for activated STATs. Direct binding assay; permeabilized cell nuclear import assay with purified proteins; dominant-negative and deletion mutant analysis The Journal of cell biology High 17178910
2006 In B lymphocytes, MgcRacGAP is required for cytokinesis and survival, but the GAP activity itself is dispensable; both the GAP domain (as a structural scaffold) and the N-terminal domain are required. A GAP-inactive mutant fully rescues the cytokinesis and survival defects of mgcRacGAP-deficient B cells. Conditional ablation of mgcRacGAP in B cell line; rescue with GAP-inactive mutant and deletion mutants Experimental cell research Medium 16959247
2007 Each subunit of the centralspindlin complex (CYK-4/MgcRacGAP and ZEN-4/MKLP1) dimerizes via a parallel coiled coil, and the two homodimers assemble into a heterotetrameric complex via two low-affinity interactions. Centralspindlin (but not individual subunits) is sufficient to bundle microtubules in vitro. Conditional mutations in the assembly interface are suppressed by second-site mutations in the interacting regions. Biochemical reconstitution; microtubule bundling assay in vitro; genetic suppressor analysis; conditional mutations Molecular biology of the cell High 17942600
2007 MgcRacGAP binds to HIF-1alpha and inhibits its transcriptional activity without lowering HIF-1alpha protein levels or altering its subcellular localization. This inhibition is dependent on the MgcRacGAP domain that interacts with HIF-1alpha, as confirmed by in vitro binding and in vivo co-immunoprecipitation. Yeast two-hybrid; in vitro binding; co-immunoprecipitation; luciferase reporter for HIF-1 transcriptional activity; overexpression with domain mutants Cellular physiology and biochemistry Medium 17982282
2008 MgcRacGAP is phosphorylated by both Aurora B and Cdk1 during mitosis. PP2A (via its B56epsilon regulatory subunit, a novel MgcRacGAP partner) dephosphorylates these phosphorylated sites. Inhibition of PP2A abrogates MgcRacGAP/Ect2 interaction, indicating PP2A-mediated dephosphorylation of MgcRacGAP is required for its interaction with Ect2 during cytokinesis. Co-immunoprecipitation; in vitro phosphorylation assay; PP2A inhibition; identification of B56epsilon as partner FEBS letters Medium 18201571
2009 MgcRacGAP functions as an NLS-containing nuclear chaperone for activated STATs: an NLS-deficient MgcRacGAP mutant blocks p-STAT nuclear translocation. MgcRacGAP also mediates STAT tyrosine phosphorylation after cytokine stimulation; STAT mutants lacking the MgcRacGAP binding site (strand betab) are barely phosphorylated. Deletion mutants in the betab-betac loop region became constitutively active with enhanced MgcRacGAP binding. NLS-deletion mutant in vitro and in vivo import assays; cytokine stimulation with phospho-STAT western blot; STAT domain deletion mutants; computer-assisted structural modeling Molecular and cellular biology Medium 19158271
2009 In v-Src-transformed NIH3T3 cells, MgcRacGAP is constitutively phosphorylated on Ser387 in interphase (cytoplasm), unlike in parental or H-RasV12-transformed cells. pS387 levels correlate with soft agar colony-forming ability. A Rac1 inhibitor (but not Aurora B inhibitor) blocks S387 phosphorylation in v-Src cells, suggesting a pathological Rac1-driven positive feedback loop that maintains pS387-MgcRacGAP in oncogenic transformation. Phospho-specific antibody; soft agar colony assay; kinase inhibitor treatment; Rac1 inhibitor treatment Cancer science Medium 19555392
2013 MgcRacGAP is degraded by the ubiquitin-proteasome pathway via APC(CDH1) in late M to G1 phase. The critical degron is located in the C-terminus (AA 537-570) of MgcRacGAP, and a PEST domain-like structure is implicated in efficient ubiquitination. Deletion mutants fused to mVenus; cell cycle synchronization; proteasome inhibitor treatment; CDH1 overexpression; degron mapping PloS one Medium 23696789
2013 MgcRacGAP inhibits HIF-1 transcriptional activity by competing with ARNT for binding to the PAS-B domain of HIF-1alpha, thereby blocking HIF-1alpha dimerization with ARNT. The Myo domain of MgcRacGAP is both necessary and sufficient for this inhibition. MgcRacGAP binding to HIF-1alpha does not affect the related factor HIF-2. In vitro pull-down assays; ARNT overexpression competition assay; HIF-1 reporter assay; domain deletion mutants Biochimica et biophysica acta Medium 23458834
2013 RacGAP1, when phosphorylated downstream of RCP-dependent α5β1 integrin trafficking and PKB/Akt signaling, is recruited to IQGAP1 at the tips of invasive pseudopods, where it locally suppresses Rac activity and promotes RhoA activity. This Rac-to-RhoA switch promotes pseudopodial extension and invasive migration into fibronectin-containing matrices. Co-immunoprecipitation; immunofluorescence localization; siRNA knockdown; active GTPase pull-down assay; invasion assays The Journal of cell biology Medium 24019536
2013 RacGAP1 is identified as a novel IQGAP1 binding partner at active β1 integrin complexes via mass spectrometry and co-immunoprecipitation. RacGAP1 is part of a filamin-A/IQGAP1/RacGAP1 complex recruited to active β1 integrin, and RacGAP1 suppression elevates Rac1 activity during cell spreading, impairing directional migration. Proteomic analysis of integrin adhesion complexes; co-immunoprecipitation; siRNA knockdown; active Rac1 pull-down; directional migration assay Journal of cell science Medium 23843620
2013 MgcRacGAP forms a complex and directly interacts in vitro with cingulin (CGN) and paracingulin (CGNL1) at tight junctions. Loss of both CGN and CGNL1 reduces MgcRacGAP expression, and exogenous MgcRacGAP rescues Rac1 activation and tight junction barrier defects in double-KD cells, establishing MgcRacGAP as a downstream effector of CGN/CGNL1 for spatially restricting Rac1 at TJs. Co-immunoprecipitation; in vitro direct binding assay; siRNA double-knockdown; Rac1 activity assay; barrier function assay Molecular biology of the cell Medium 24807907
2013 Crystal structure of the GTPase-activating protein (GAP) domain of MgcRacGAP was determined at 1.9 Å resolution. The conformation of the catalytic arginine finger (Arg385) differs from previously reported GAP proteins. The GAP domain (residues 348-546) exists as a monomer in solution. Mutant GAP activity measurements toward Rac1 were performed. X-ray crystallography (1.9 Å); size exclusion chromatography for oligomeric state; in vitro GAP activity assay with mutants Biochemical and biophysical research communications High 23665020
2013 Male germ cell-specific deletion of MgcRacGAP in mice using Stra8-Cre causes failure to form intercellular bridges between germ cells (which normally do not complete cytokinesis), leading to germline depletion, proliferation arrest, and male sterility. This establishes MgcRacGAP's role in intercellular bridge formation during spermatogenesis. Conditional knockout mouse (Stra8-Cre); histological analysis; immunostaining for intercellular bridges Developmental biology High 24355749
2014 Polo-like kinase 1 (Plk1) phosphorylates MgcRacGAP at two sites, S157 and S164. Phosphorylation of S157 alone is necessary but not sufficient for Ect2 BRCT domain binding; phosphorylation of S164 is additionally required for efficient binding. Furthermore, MKLP1 (centralspindlin assembly) is needed for BRCT binding, establishing that centralspindlin assembly and two Plk1-dependent phosphorylations together initiate Ect2 recruitment in early cytokinesis. Phosphorylation site mapping; binding assays with BRCT domain; mutagenesis of S157 and S164; MKLP1 depletion Cell cycle Medium 25486482
2014 RacGAP1 promotes RhoA activation in endothelial cells, triggering FAK and paxillin activation and focal adhesion formation, which disrupts adherens junctions and promotes melanoma cell transendothelial migration. A RacGAP1 mutant (T249A) and RacGAP1 siRNA attenuate these effects. siRNA knockdown; RacGAP1 mutant overexpression; RhoA activity assay; focal adhesion staining; transendothelial migration assay Biochemical and biophysical research communications Medium 25475728
2014 Trio is identified as a mitotic GEF for Rac1 that counteracts MgcRacGAP function during cytokinesis. Trio depletion rescues cytokinesis failure induced by MgcRacGAP depletion, and this rescue is mediated by the Trio-Rac1 pathway (blocked by GEF-dead Trio mutants and Rac1 inhibitor), establishing a Trio (Rac1 activator) vs. MgcRacGAP (Rac1 inactivator) antagonism at the cleavage furrow. siRNA screen; RNAi epistasis (double depletion); GEF-dead Trio mutant; Rac1 activity assay; cytokinesis failure quantification Molecular biology of the cell Medium 25355950
2015 CYK-4/MgcRacGAP RhoGAP activity promotes RhoA activation (rather than inactivation) during cytokinesis by a non-canonical mechanism: CYK-4 must localize to the plasma membrane, bind RhoA, and promote GTP hydrolysis by RhoA to activate ECT-2. The catalytic domains of CYK-4 and ECT-2 directly interact, and defects from loss of CYK-4 RhoGAP activity are rescued by activating ECT-2 mutations or depletion of the canonical RhoA GAP RGA-3/4. C. elegans genetics; in vitro direct interaction of CYK-4 and ECT-2 catalytic domains; suppressor mutations in ECT-2; RGA-3/4 depletion epistasis; plasma membrane localization assays eLife High 26252513
2015 In Xenopus laevis epithelia, MgcRacGAP's GAP activity restricts RhoA-GTP at the cleavage furrow and restricts both RhoA-GTP and Rac1-GTP at cell-cell junctions. Phosphorylation at Ser-386 does not switch MgcRacGAP's GAP substrate specificity and is not required for successful cytokinesis. Mgc regulates adherens junction structure via its GAP activity through the RhoA pathway. Xenopus laevis embryo injections with GAP-dead and S386A/D mutants; FRET biosensors for active RhoA/Rac1; adherens junction immunostaining Molecular biology of the cell Medium 25947135
2016 Progressive loss of RacGAP1 in zebrafish (ogre mutant) reveals that RacGAP1 activity controls sequential aspects of cytokinesis: graded reduction causes first abscission failure, then cleavage furrow ingression failure, and finally complete absence of furrow formation, demonstrating a dose-dependent role in different steps of cytokinesis. Zebrafish maternal/zygotic loss-of-function mutant; in vivo cell recording; live imaging Developmental biology Medium 27339293
2017 MgcRacGAP contains a conserved SxIP motif that tethers centralspindlin to EB1/EB3 on microtubule plus ends in Xenopus laevis. Mutation of the SxIP motif abolishes MgcRacGAP tracking on growing microtubule plus ends, causing abnormal astral microtubule organization, mislocalization of MgcRacGAP to the polar cortex (away from contractile ring), mislocalization of RhoA, and severe cytokinesis defects and adherens junction perturbation. SxIP motif mutagenesis; live cell imaging of EB3 tracking; immunofluorescence of RhoA and downstream targets; cytokinesis quantification in Xenopus embryos Journal of cell science Medium 28389580
2019 RACGAP1 induces STAT3 phosphorylation and promotes its nuclear translocation in bladder cancer, establishing a RACGAP1→STAT3 signaling axis. In turn, p-STAT3 promotes DNMT3B recruitment to the ESR1 promoter causing its methylation and silencing, while ESR1 normally drives miR-4324 expression that suppresses RACGAP1, completing a feedback loop. Ectopic overexpression/knockdown; STAT3 phosphorylation western blot; nuclear translocation immunofluorescence; ChIP assay for DNMT3B at ESR1 promoter; promoter methylation analysis International journal of cancer Medium 30511377
2021 RACGAP1 promotes mitochondrial fission by recruiting ECT2 during anaphase and activating the ERK-DRP1 pathway. Phosphorylation of RACGAP1 is essential for its ability to bind ECT2 and exert downstream effects on mitochondrial dynamics. RACGAP1 overexpression also increases PGC-1a expression (presumably via increased mitophagy intensity), augmenting mitochondrial biogenesis. Co-immunoprecipitation; mitochondrial morphology imaging; mitophagy assay; glycolysis/ATP measurement; DRP1 phosphorylation western blot; overexpression and knockdown Experimental cell research Low 33485843
2023 RACGAP1 promotes neuroendocrine transdifferentiation of prostate cancer by stabilizing EZH2 expression via the ubiquitin-proteasome pathway. E2F1 transcriptionally induces RACGAP1 expression (confirmed by luciferase reporter and ChIP assays). RACGAP1 interacts with EZH2 (confirmed by co-immunoprecipitation) and prevents its ubiquitin-proteasome-dependent degradation. Co-immunoprecipitation; luciferase reporter assay; ChIP for E2F1 binding to RACGAP1 promoter; ubiquitin-proteasome pathway assays; western blot Aging and disease Medium 37196108
2024 Crystal structures of the MgcRacGAP GAP domain complexed with CDC42·GDP·AlF4- (wild-type) and with RHOA·GDP·AlF4- (S378D phosphomimetic mutant fusion) were determined. The S387D mutation reduces interactions with CDC42 more severely than with RHOA, decreasing GAP activity toward CDC42 while having only moderate impact on RHOA, providing structural basis for the substrate preference shift upon Ser387 phosphorylation. X-ray crystallography of GAP domain complexes with GTPases; in vitro GAP activity assays of S387D and S387A mutants Journal of structural biology High 39522789
2024 AR (androgen receptor) transcriptionally activates RACGAP1 expression by binding to its promoter. Reciprocally, nuclear RACGAP1 binds to the N-terminal domain (NTD) of both AR and AR-V7, blocking their interaction with the E3 ubiquitin ligase MDM2 and preventing their ubiquitin-proteasome-dependent degradation. This positive feedback loop contributes to endocrine therapy resistance. ChIP for AR binding to RACGAP1 promoter; co-immunoprecipitation of RACGAP1 with AR/AR-V7; ubiquitination assay; domain mapping (NTD); in vivo xenograft model with siRNA Cell communication and signaling Medium 38898473
2025 In a membrane-reconstituted system, RacGAP1 binds membranes through both its C1 domain and GAP domain cooperatively, with PS as a major lipid required in addition to PIP2. Membranes potentiate RacGAP1 GAP activity toward Rac1 but do not alter its marked specificity for Rac1 over RhoA. The Rac1 switch 1 region and insert region are identified by mutagenesis as determinants of this selectivity. Crystal structure of the Rac1-GDP-Pi complex was determined. Liposome reconstitution; fluorescence-based kinetic GAP assay on membranes; crystal structure of Rac1-GDP-Pi; mutagenesis of Rac1 specificity determinants Protein science High 41676911
2025 MARCH5 E3 ubiquitin ligase promotes ubiquitination of RACGAP1, leading to its degradation, which prevents excessive DRP1-mediated mitochondrial fission. Loss of MARCH5 increases RACGAP1 levels, activates DRP1, and impairs mitochondrial quality control, contributing to aortic valve calcification. Co-immunoprecipitation and mass spectrometry confirmed MARCH5-RACGAP1 interaction. Co-immunoprecipitation; mass spectrometry; ubiquitination assay; RACGAP1 inhibition rescue experiment; mitochondrial morphology analysis; in vivo mouse model Biochimica et biophysica acta. Molecular cell research Medium 39880131
2024 Using lipid-trap mass spectrometry (LTMS), RACGAP1 was found to associate with specific lipid species in dividing HeLa cells compared to non-dividing cells, indicating cell division-specific lipid-protein interactions for RACGAP1. Lipid-trap mass spectrometry (immunoprecipitation of GFP-tagged RACGAP1 followed by lipidomic analysis) bioRxivpreprint Low

Source papers

Stage 0 corpus · 93 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis. Developmental cell 252 12689593
2005 MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis. Proceedings of the National Academy of Sciences of the United States of America 178 16129829
2000 MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody. The Journal of biological chemistry 160 11085985
1998 MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells. The Journal of biological chemistry 144 9497316
2013 RCP-driven α5β1 recycling suppresses Rac and promotes RhoA activity via the RacGAP1-IQGAP1 complex. The Journal of cell biology 115 24019536
2007 Cooperative assembly of CYK-4/MgcRacGAP and ZEN-4/MKLP1 to form the centralspindlin complex. Molecular biology of the cell 95 17942600
2005 Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis. The Journal of cell biology 93 15642749
2006 Rac1 and a GTPase-activating protein, MgcRacGAP, are required for nuclear translocation of STAT transcription factors. The Journal of cell biology 89 17178910
2005 Inhibition of cyclin-dependent kinase 1 induces cytokinesis without chromosome segregation in an ECT2 and MgcRacGAP-dependent manner. The Journal of biological chemistry 76 16118207
2014 Clinical significance of RacGAP1 expression at the invasive front of gastric cancer. Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association 74 24615626
2015 The RhoGAP activity of CYK-4/MgcRacGAP functions non-canonically by promoting RhoA activation during cytokinesis. eLife 71 26252513
2004 Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase. The Journal of biological chemistry 71 14744859
2009 A Rac GTPase-activating protein, MgcRacGAP, is a nuclear localizing signal-containing nuclear chaperone in the activation of STAT transcription factors. Molecular and cellular biology 68 19158271
2012 Validity of the proliferation markers Ki67, TOP2A, and RacGAP1 in molecular subgroups of breast cancer. Breast cancer research and treatment 64 23135572
2013 Rac1 is deactivated at integrin activation sites through an IQGAP1-filamin-A-RacGAP1 pathway. Journal of cell science 60 23843620
2019 miR-4324-RACGAP1-STAT3-ESR1 feedback loop inhibits proliferation and metastasis of bladder cancer. International journal of cancer 59 30511377
2000 MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells. Blood 56 10979956
2021 RACGAP1 modulates ECT2-Dependent mitochondrial quality control to drive breast cancer metastasis. Experimental cell research 44 33485843
2019 lncRNA MAGI2-AS3 Prevents the Development of HCC via Recruiting KDM1A and Promoting H3K4me2 Demethylation of the RACGAP1 Promoter. Molecular therapy. Nucleic acids 43 31629962
2015 MgcRacGAP restricts active RhoA at the cytokinetic furrow and both RhoA and Rac1 at cell-cell junctions in epithelial cells. Molecular biology of the cell 43 25947135
2014 MgcRacGAP interacts with cingulin and paracingulin to regulate Rac1 activation and development of the tight junction barrier during epithelial junction assembly. Molecular biology of the cell 43 24807907
2008 CUX1 and E2F1 regulate coordinated expression of the mitotic complex genes Ect2, MgcRacGAP, and MKLP1 in S phase. Molecular and cellular biology 43 19015243
2016 RNA-seq Identification of RACGAP1 as a Metastatic Driver in Uterine Carcinosarcoma. Clinical cancer research : an official journal of the American Association for Cancer Research 41 27121792
2012 Analysis of 20 genes at chromosome band 12q13: RACGAP1 and MCRS1 overexpression in nonsmall-cell lung cancer. Genes, chromosomes & cancer 40 23225332
2004 MgcRacGAP regulates cortical activity through RhoA during cytokinesis. Experimental cell research 37 14729465
2016 Filling GAPs in our knowledge: ARHGAP11A and RACGAP1 act as oncogenes in basal-like breast cancers. Small GTPases 36 27657701
2001 Mice with a homozygous gene trap vector insertion in mgcRacGAP die during pre-implantation development. Mechanisms of development 35 11287179
2013 Expression of RACGAP1 in high grade meningiomas: a potential role in cancer progression. Journal of neuro-oncology 34 23525949
2007 MgcRacGAP interacts with HIF-1alpha and regulates its transcriptional activity. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 34 17982282
2008 Phosphoregulation of MgcRacGAP in mitosis involves Aurora B and Cdk1 protein kinases and the PP2A phosphatase. FEBS letters 33 18201571
2019 Pseudogene RACGAP1P activates RACGAP1/Rho/ERK signalling axis as a competing endogenous RNA to promote hepatocellular carcinoma early recurrence. Cell death & disease 31 31160556
2006 Regulation of cytokinesis by mgcRacGAP in B lymphocytes is independent of GAP activity. Experimental cell research 31 16959247
2003 Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells. The Biochemical journal 31 12590651
2020 Long non-coding RNA RACGAP1P promotes breast cancer invasion and metastasis via miR-345-5p/RACGAP1-mediated mitochondrial fission. Molecular oncology 29 33252198
2016 Comparative evaluation of three proliferation markers, Ki-67, TOP2A, and RacGAP1, in bronchopulmonary neuroendocrine neoplasms: Issues and prospects. Oncotarget 29 27259241
2019 Gene Regulation by Antitumor miR-204-5p in Pancreatic Ductal Adenocarcinoma: The Clinical Significance of Direct RACGAP1 Regulation. Cancers 27 30866526
2023 Overexpression of RACGAP1 by E2F1 Promotes Neuroendocrine Differentiation of Prostate Cancer by Stabilizing EZH2 Expression. Aging and disease 26 37196108
2023 PLAGL2 promotes bladder cancer progression via RACGAP1/RhoA GTPase/YAP1 signaling. Cell death & disease 23 37454211
2022 EGF-induced nuclear translocation of SHCBP1 promotes bladder cancer progression through inhibiting RACGAP1-mediated RAC1 inactivation. Cell death & disease 23 35013128
2016 Clinicopathological Significance of the Proliferation Markers Ki67, RacGAP1, and Topoisomerase 2 Alpha in Breast Cancer. International journal of surgical pathology 23 27284123
2014 Centralspindlin assembly and 2 phosphorylations on MgcRacGAP by Polo-like kinase 1 initiate Ect2 binding in early cytokinesis. Cell cycle (Georgetown, Tex.) 22 25486482
2001 Role of MgcRacGAP/Cyk4 as a regulator of the small GTPase Rho family in cytokinesis and cell differentiation. Cell structure and function 21 11942621
2022 RacGAP1 promotes the malignant progression of cervical cancer by regulating AP-1 via miR-192 and p-JNK. Cell death & disease 20 35831303
2022 Up-Regulation of RACGAP1 Promotes Progressions of Hepatocellular Carcinoma Regulated by GABPA via PI3K/AKT Pathway. Oxidative medicine and cellular longevity 20 35958019
2022 PRC1 and RACGAP1 are Diagnostic Biomarkers of Early HCC and PRC1 Drives Self-Renewal of Liver Cancer Stem Cells. Frontiers in cell and developmental biology 19 35445033
2016 Expression of aurora kinase A correlates with the Wnt-modulator RACGAP1 in gastric cancer. Cancer medicine 19 26778597
2023 m6A-modified circASXL1 promotes proliferation and migration of ovarian cancer through the miR-320d/RACGAP1 axis. Carcinogenesis 17 37738681
2019 Rac GTPase-Activating Protein 1 (RACGAP1) as an Oncogenic Enhancer in Esophageal Carcinoma. Oncology 15 31216559
2016 Progressive loss of RacGAP1/ogre activity has sequential effects on cytokinesis and zebrafish development. Developmental biology 15 27339293
2014 Identification of a mitotic Rac-GEF, Trio, that counteracts MgcRacGAP function during cytokinesis. Molecular biology of the cell 15 25355950
2014 RacGAP1-driven focal adhesion formation promotes melanoma transendothelial migration through mediating adherens junction disassembly. Biochemical and biophysical research communications 15 25475728
2013 APC(CDH1) targets MgcRacGAP for destruction in the late M phase. PloS one 14 23696789
2013 Deletion of MgcRacGAP in the male germ cells impairs spermatogenesis and causes male sterility in the mouse. Developmental biology 14 24355749
1999 Structure and expression of murine mgcRacGAP: its developmental regulation suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis. The Biochemical journal 14 10493933
2020 RacGAP1 ameliorates acute kidney injury by promoting proliferation and suppressing apoptosis of renal tubular cells. Biochemical and biophysical research communications 13 32423815
2017 Temporal regulation of epithelium formation mediated by FoxA, MKLP1, MgcRacGAP, and PAR-6. Molecular biology of the cell 13 28539408
2022 Effects of Shenkang Pills on Early-Stage Diabetic Nephropathy in db/db Mice via Inhibiting AURKB/RacGAP1/RhoA Signaling Pathway. Frontiers in pharmacology 12 35222021
2022 RACGAP1 promotes proliferation and cell cycle progression by regulating CDC25C in cervical cancer cells. Tissue & cell 12 35489195
2024 Reciprocal regulation between RACGAP1 and AR contributes to endocrine therapy resistance in prostate cancer. Cell communication and signaling : CCS 11 38898473
2017 The MgcRacGAP SxIP motif tethers Centralspindlin to microtubule plus ends in Xenopus laevis. Journal of cell science 11 28389580
2008 Essential roles of mgcRacGAP in multilineage differentiation and survival of murine hematopoietic cells. Biochemical and biophysical research communications 11 18541143
2024 FOXM1 transcriptional regulation of RacGAP1 activates the PI3K/AKT signaling pathway to promote the proliferation, migration, and invasion of cervical cancer cells. International journal of clinical oncology 10 38172354
2020 RACGAP1 is transcriptionally regulated by E2F3, and its depletion leads to mitotic catastrophe in esophageal squamous cell carcinoma. Annals of translational medicine 10 32953750
2015 Discovery of MINC1, a GTPase-activating protein small molecule inhibitor, targeting MgcRacGAP. Combinatorial chemistry & high throughput screening 10 25479424
2013 MgcRacGAP, a cytoskeleton regulator, inhibits HIF-1 transcriptional activity by blocking its dimerization. Biochimica et biophysica acta 10 23458834
2019 Lambda-Carrageenan Enhances the Effects of Radiation Therapy in Cancer Treatment by Suppressing Cancer Cell Invasion and Metastasis through Racgap1 Inhibition. Cancers 9 31426369
2015 MgcRacGAP inhibition stimulates JAK-dependent STAT3 activity. FEBS letters 9 26602080
2024 RACGAP1 promotes lung cancer cell proliferation through the PI3K/AKT signaling pathway. Scientific reports 8 38622149
2024 The Expression Regulation and Cancer-Promoting Roles of RACGAP1. Biomolecules 8 39858398
2022 LncRNA PART1 Stimulates the Development of Ovarian Cancer by Up-regulating RACGAP1 and RRM2. Reproductive sciences (Thousand Oaks, Calif.) 8 35553409
2018 Admixture Mapping Links RACGAP1 Regulation to Prostate Cancer in African Americans. Cancer genomics & proteomics 8 29695400
2024 RACGAP1 drives proliferation, migration and invasion and suppresses autophagy of gastric cancer cells via inhibiting SIRT1/Mfn2. Physiology international 6 38261006
2009 Constitutive phosphorylation of a Rac GAP MgcRacGAP is implicated in v-Src-induced transformation of NIH3T3 cells. Cancer science 6 19555392
2023 HIF‑1α and RACGAP1 promote the progression of hepatocellular carcinoma in a mutually regulatory way. Molecular medicine reports 5 37772389
2017 Proliferation markers RacGAP1 and Ki-67 in gastrointestinal stromal tumors by immunohistochemistry with respect to clinicopathological features and different risk stratification systems. International journal of clinical and experimental pathology 5 31966533
2013 Crystal structure of GTPase-activating domain from human MgcRacGAP. Biochemical and biophysical research communications 5 23665020
2023 Oncogenic and immunological roles of RACGAP1 in pan-cancer and its potential value in nasopharyngeal carcinoma. Apoptosis : an international journal on programmed cell death 4 37670104
2023 Racgap1 knockdown results in cells with multiple cilia due to cytokinesis failure. Annals of human genetics 4 37771269
2018 Tangshen Formula Treatment for Diabetic Kidney Disease by Inhibiting Racgap1-stata5-Mediated Cell Proliferation and Restoring miR-669j-Arntl-Related Circadian Rhythm. Medical science monitor : international medical journal of experimental and clinical research 4 30394366
2025 RACGAP1 promotes tumor progression by influencing neutrophil recruitment and tumor cell proliferation in colorectal cancer. Journal of immunology (Baltimore, Md. : 1950) 2 40504027
2024 RACGAP1 knockdown synergizes and enhances the effects of chemotherapeutics on ovarian cancer. American journal of translational research 2 38883382
2024 Structural basis for the effects of Ser387 phosphorylation of MgcRacGAP on its GTPase-activating activities for CDC42 and RHOA. Journal of structural biology 2 39522789
2025 RacGAP1 Plays an Oncogenic Role in Lung Adenocarcinoma by Regulating the Wnt/β-Catenin Pathway. Cells 1 40497948
2025 Nanoparticle-mediated overexpression of RacGAP1 protects against renal ischemia/reperfusion injury by maintaining mitochondrial homeostasis. Clinical science (London, England : 1979) 1 41230850
2025 Inhibition of RACGAP1 sensitizes triple-negative breast cancer cells to ferroptosis by regulating CPT1A-dependent fatty acid metabolism. Journal of experimental & clinical cancer research : CR 1 41444950
2024 Targeting RACGAP1 suppresses growth hormone pituitary adenoma growth. Endocrine 1 39607642
2026 RACGAP1 defines a malignant proliferative niche and represents a therapeutic vulnerability in lung adenocarcinoma. Translational lung cancer research 0 41659265
2026 The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes. Protein science : a publication of the Protein Society 0 41676911
2025 MARCH5 ameliorates aortic valve calcification via RACGAP1-DRP1 associated mitochondrial quality control. Biochimica et biophysica acta. Molecular cell research 0 39880131
2025 Biological and metabolomic insights into RACGAP1-mediated growth and progression of clear cell renal cell carcinoma. American journal of physiology. Cell physiology 0 40522863
2025 Rho GAPase protein 1 (RACGAP1) affects the proliferation and metastasis of esophageal squamous cell carcinoma cells by regulating signaling pathways: Thermal infrared medical image inspection. Journal of thermal biology 0 40561732
2025 MCM7 promotes liver fibrosis by transcriptionally regulating IL11 via the SHCBP1-RACGAP1-STAT3 axis. Cell death & disease 0 40789837
2025 RACGAP1 promotes the malignant phenotype and cisplatin resistance of nasopharyngeal carcinoma cells by upregulating HIF-1α. Journal of chemotherapy (Florence, Italy) 0 41236483

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