Affinage

GIT2

ARF GTPase-activating protein GIT2 · UniProt Q14161

Length
759 aa
Mass
84.5 kDa
Annotated
2026-06-10
42 papers in source corpus 21 papers cited in narrative 21 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

GIT2 is a multifunctional ARF GTPase-activating protein that operates as a signaling scaffold coupling cytoskeletal remodeling to cell migration, immune signaling, and genome maintenance (PMID:10896954, PMID:16628223). Through its ARF-GAP domain it inactivates ARF1 to control Golgi organization and focal adhesion/actin architecture, an activity that is catalytically required for these effects (PMID:11251077). GIT2 nucleates a paxillin–β-PIX–PAK1 complex—binding paxillin via the LD4 motif to localize at focal contacts—and integrates this module with Crk/CrkL adaptors, the Rac1 GEF Vav2, and DOCK5 to spatiotemporally restrain Rac1 and Cdc42 activity; loss of GIT2 produces sustained Rac activation, excess lamellipodia, faster focal adhesion turnover, and loss of directional motility (PMID:11448998, PMID:11157752, PMID:12857867, PMID:16628223, PMID:23615439, PMID:27669437). Consistent with a brake on Rac-driven motility, GIT2 acts downstream of Gβγ and CXCR2 to enforce directional chemotaxis and suppress superoxide in neutrophils, governs thymocyte selection and migration, and controls myosin II-mediated contractility during gastrulation (PMID:16715100, PMID:20431621, PMID:21034731, PMID:29229683). Beyond the cytoskeleton, GIT2 is a negative regulator of inflammatory signaling: it recruits the deubiquitinase CYLD to remove K63-linked ubiquitin from TRAF6 to terminate TLR-induced NF-κB/MAPK signaling, and directly binds the NF-κB subunits p65 and p52 while elevating TRAF3 to suppress canonical and non-canonical NF-κB output (PMID:24879442, PMID:39954559). A nuclear pool of GIT2 is phosphorylated by ATM and recruited to DNA double-strand breaks in an H2AX/MRE11-dependent manner, where it stabilizes BRCA1 and promotes repair (PMID:25605334). PKC-mediated phosphorylation at S46 in the ArfGAP domain drives centrosomal localization where GIT2 negatively regulates γ-tubulin-dependent microtubule nucleation (PMID:38370406, PMID:40176062).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2000 High

    Established GIT2's core biochemical identity by showing it is an ARF1-directed GAP that also binds GRK2 and PIX-PAK complexes and regulates receptor sequestration, defining it as both an enzyme and a scaffold.

    Evidence In vitro GAP assay, co-immunoprecipitation, and receptor sequestration readout across splice variants

    PMID:10896954

    Open questions at the time
    • Cellular substrate specificity beyond ARF1 not defined
    • Functional distinction between long/short variants only assayed via receptor sequestration
  2. 2001 High

    Defined how GIT2 reaches focal adhesions and what it does there—paxillin LD4 binding targets it to focal contacts to restrain Rac and enforce directional motility, while its GAP activity reorganizes Golgi and adhesions.

    Evidence Reciprocal deletion mutants in fibroblasts, GAP-inactive mutant rescue, immunofluorescence and Rac/motility assays

    PMID:11251077 PMID:11448998

    Open questions at the time
    • Direct in vivo ARF1 GTP-loading not measured
    • Link between Golgi reorganization and motility phenotype not mechanistically connected
  3. 2001 High

    Showed the PAK1–β-PIX–GIT2 module is a stable trimolecular complex activated downstream of receptor signaling, placing PIX GEF activity within the complex upstream of Rho/PAK.

    Evidence Co-IP and dominant-negative PIX in TCR-stimulated Jurkat cells with kinase inhibitors and adaptor-null lines

    PMID:11157752

    Open questions at the time
    • Stoichiometry of the complex not determined
    • Direct GIT2 contribution to complex assembly versus PIX/PAK not isolated
  4. 2003 High

    Integrated Crk/CrkL adaptors into the paxillin/GIT2/β-PIX complex, linking the scaffold to Rac-dependent paxillin relocalization and lamellipodia formation.

    Evidence Reciprocal Co-IP, dominant-negative Crk mutants, Rac inhibition, immunofluorescence

    PMID:12857867

    Open questions at the time
    • Direct versus indirect Crk-GIT2 contact not resolved
    • Quantitative ordering of complex assembly steps unknown
  5. 2006 High

    Demonstrated endogenous GIT2 is a brake on motility, repressing lamellipodia via Rac1 and focal adhesion turnover via Cdc42 with Crk as the essential effector and β-PIX dispensable, refining the pathway logic.

    Evidence siRNA knockdown in MCF10A epithelial cells with epistasis across Rac1, Cdc42, Crk, β-PIX

    PMID:16628223

    Open questions at the time
    • Mechanism by which GIT2 selectively suppresses Crk not defined
    • Why β-PIX is dispensable here but required in other contexts unresolved
  6. 2006 High

    Extended GIT2's motility-suppressing role into innate immunity in vivo, showing it acts downstream of Gβγ and upstream of ARF1 to direct neutrophil chemotaxis and limit superoxide, with knockout causing immunodeficiency.

    Evidence GIT2-knockout mouse neutrophils, chemotaxis and superoxide assays, epistasis

    PMID:16715100

    Open questions at the time
    • Molecular link between Gβγ and GIT2 recruitment not identified
    • Mechanism of superoxide suppression not detailed
  7. 2010 High

    Confirmed conserved GIT2 control of cell movement in distinct in vivo systems—negatively regulating Rac-driven thymocyte motility and controlling myosin II contractility via MLC phosphorylation in gastrulation.

    Evidence Git2-knockout mice with intravital two-photon imaging; zebrafish morpholino with chicken GIT2 rescue and MLC phosphorylation/blebbistatin assays

    PMID:20431621 PMID:21034731

    Open questions at the time
    • How GIT2 regulates MLC phosphorylation mechanistically unknown
    • Connection between Rac suppression and contractility control not unified
  8. 2013 High

    Identified a phosphorylation-dependent GIT2-Vav2 feedforward loop downstream of integrin and EGF that controls Rac1 activation and directional persistence, and linked GIT2 loss to EMT via a miR-146a/Cnot6L/Zeb1 axis.

    Evidence Co-IP, knockdown of both partners, Rac1 assays, migration directionality; separate miR-146a maturation and Zeb1 mRNA stability assays

    PMID:23591815 PMID:23615439

    Open questions at the time
    • Kinase phosphorylating GIT2 to drive Vav2 interaction not identified
    • EMT/miR-146a axis is Medium-confidence and pathway not independently confirmed
  9. 2014 High

    Revealed a non-cytoskeletal role: GIT2 terminates TLR-induced NF-κB/MAPK signaling by recruiting CYLD to deubiquitinate TRAF6, establishing it as a negative regulator of inflammation.

    Evidence Git2-knockout mice/macrophages, TLR stimulation, GIT2-CYLD Co-IP, TRAF6 ubiquitination assay

    PMID:24879442

    Open questions at the time
    • Whether ARF-GAP activity is required for CYLD recruitment unknown
    • Direct GIT2-TRAF6 contact not established
  10. 2015 High

    Placed GIT2 in genome maintenance, showing a nuclear pool is phosphorylated by ATM and recruited to DSBs via H2AX/ATM/MRE11 to stabilize BRCA1 and promote repair.

    Evidence Nuclear fractionation, Co-IP with DDR factors, ATM kinase assay, dependency analysis, GIT2-KO mouse irradiation

    PMID:25605334

    Open questions at the time
    • ATM phosphorylation sites not mapped
    • How a cytoskeletal scaffold mechanistically stabilizes BRCA1 unresolved
  11. 2016 High

    Refined the migration machinery and GIT2 regulation: GIT2 restrains DOCK5-Crk-p130Cas signaling and FA turnover under Rho-ROCK contractility, while RUSC2 (and Rab35) and the insulin receptor/IRS-2 control GIT2 stability and tissue-specific functions.

    Evidence Co-IP of GIT2-DOCK5-Crk, ROCK/MLC inhibition, invasion assays; RUSC2/Rab35 silencing and stability assays; GIT2-IR/IRS-2 Co-IP and KO mouse metabolic phenotyping

    PMID:26834700 PMID:27238570 PMID:27669437

    Open questions at the time
    • RUSC2 and insulin receptor findings are Medium-confidence and single-lab
    • Mechanism of GIT2 stabilization/degradation control incomplete
  12. 2024 High

    Established a centrosomal function distinct from GIT1: PKC phosphorylation of GIT2 at S46 in the ArfGAP domain drives centrosomal localization where GIT2 negatively regulates γ-tubulin-dependent microtubule nucleation.

    Evidence shRNA depletion, Co-IP with γTuRC components, microtubule nucleation assays, S46 mutagenesis and PKC inhibitors in mast cells and glioblastoma

    PMID:38370406 PMID:40176062

    Open questions at the time
    • Whether ARF-GAP catalytic activity is required for nucleation control unknown
    • Mechanism of negative regulation of γTuRC not defined
  13. 2025 Medium

    Extended NF-κB suppression to direct subunit binding and exposed a disease-relevant splicing axis: GIT2 binds p65 and p52 and elevates TRAF3 to suppress NF-κB and senescence, while THRAP3/SLU7-driven Exon14 skipping yields a variant conferring ferroptosis resistance in AML.

    Evidence GIT2-p65/p52 Co-IP, BMSC functional assays and ovariectomy model; THRAP3-SLU7 Co-IP, Exon14 splicing assays, ferroptosis and orthotopic tumor models

    PMID:39954559 PMID:41326370

    Open questions at the time
    • Both are Medium-confidence single-lab studies
    • Functional contribution of specific GIT2 splice variants to NF-κB and ferroptosis not reconciled

Open questions

Synthesis pass · forward-looking unresolved questions
  • How GIT2's distinct functional pools—focal adhesion scaffold, nuclear DDR factor, NF-κB suppressor, and centrosomal regulator—are coordinated, and whether its ARF-GAP catalytic activity is required for each, remains unresolved.
  • No unifying model linking cytoskeletal, nuclear, immune, and centrosomal roles
  • Catalytic requirement for non-adhesion functions untested
  • No structural model of GIT2 in any complex

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3
Localization
GO:0005794 Golgi apparatus 2 GO:0005815 microtubule organizing center 2 GO:0005856 cytoskeleton 2 GO:0005634 nucleus 1
Pathway
R-HSA-168256 Immune System 4 R-HSA-162582 Signal Transduction 3 R-HSA-1266738 Developmental Biology 1 R-HSA-73894 DNA Repair 1
Partners
ARHGEF7CRKCYLDDOCK5GRK2PAK1PXNVAV2
Complex memberships
paxillin–β-PIX–PAK1 (GIT2/PKL) complexγ-tubulin ring complex (γTuRC) association

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 GIT2 (including both long and short splice variants) possesses ARF GTPase-activating protein (ARF-GAP) activity toward ARF1 in vitro, interacts with G protein-coupled receptor kinase 2 (GRK2), and interacts with PIX-PAK complexes. The longest GIT2 variant inhibits beta2-adrenergic receptor sequestration when overexpressed, whereas the shortest splice variant is inactive in this assay. In vitro GAP assay, co-immunoprecipitation, cellular overexpression with receptor sequestration readout The Journal of biological chemistry High 10896954
2001 GIT2/PKL (paxillin kinase linker) interacts with paxillin via the paxillin LD4 motif; this interaction is required for PKL localization to focal contacts and for normal Rac-dependent cell spreading and directional motility. Loss of the paxillin-PKL interaction leads to prolonged Rac activation, multiple broad lamellipodia, and impaired directional motility without affecting FAK activity. Overexpression of deletion mutants (paxillinΔLD4, PKLδPBS2) in CHO.K1 fibroblasts; immunofluorescence localization; cell spreading/motility assays; Rac activity measurements The Journal of cell biology High 11448998
2001 GIT2-short (KIAA0148), a short isoform of GIT2, co-localizes with paxillin at perinuclear areas and acts as an ARF-GAP for ARF1 in vivo. Overexpression of wild-type GIT2-short (but not its GAP-inactive mutant) redistributes Golgi protein β-COP, reduces focal adhesions and actin stress fibers, and alters perinuclear paxillin localization, demonstrating that the ARF-GAP catalytic activity is required for these effects. Overexpression and GAP-inactive mutant rescue in cells; immunofluorescence co-localization; Golgi distribution assay; focal adhesion and actin stress fiber quantification Molecular biology of the cell High 11251077
2001 PAK1, PIX (β-PIX), and p95PKL (GIT2) form a stable trimolecular complex in T cells. This complex is activated downstream of the T-cell receptor via ZAP-70/Syk kinases and a LAT/Slp-76-independent pathway; PIX GEF activity within the complex is required for Rho GTPase activation upstream of PAK1. Co-immunoprecipitation demonstrating trimolecular complex; dominant-negative PIX overexpression; TCR stimulation assays with kinase inhibitors and adaptor-deficient Jurkat cells The EMBO journal High 11157752
2003 CrkII/CrkL adapter proteins associate with a Paxillin/GIT2/β-PIX complex; this association promotes Rac-dependent relocalization of paxillin to focal contacts and lamellipodia formation. Paxillin mutants unable to associate with Crk or GIT2 block Crk-dependent cell spreading. Co-immunoprecipitation; stable cell line overexpression; dominant-negative Crk mutants; Rac inhibition; immunofluorescence localization Molecular biology of the cell High 12857867
2006 Endogenous GIT2 represses lamellipodial extension via Rac1-dependent signaling and represses focal adhesion turnover via Cdc42-dependent signaling. GIT2 knockdown is sufficient to induce migration of non-transformed MCF10A epithelial cells. The SH2-SH3 adaptor Crk is identified as an essential downstream target of GIT2 inhibition, whereas β-PIX is dispensable for GIT2-mediated effects. siRNA knockdown of endogenous GIT2; lamellipodia and FA turnover assays; epistasis with Rac1, Cdc42, Crk, and β-PIX The EMBO journal High 16628223
2006 GIT2 is required in neutrophils for directional chemotaxis and for suppression of superoxide production in response to G protein-coupled receptor stimulation. GIT2 suppresses ARF1 activity and functions downstream of Gβγ subunits in the direction-sensing machinery. Loss of GIT2 in vivo leads to an immunodeficient state. GIT2-knockout mouse neutrophils; directional chemotaxis assays; superoxide production measurements; epistasis placing GIT2 downstream of Gβγ and upstream of ARF1 Nature immunology High 16715100
2010 GIT2 is required for efficient thymocyte positive selection. Git2-/- double-positive thymocytes show elevated Rac GTPase activation, increased actin polymerization, and enhanced chemokine-directed migration in vitro. Two-photon microscopy revealed that scanning activity of Git2-/- thymocytes was compromised in the thymic cortex, indicating GIT2 negatively regulates Rac-mediated chemotactic motility in thymocytes. Git2-knockout mice; Rac activation assay; actin polymerization assay; in vitro chemotaxis; two-photon laser-scanning microscopy in intact thymus Nature immunology High 20431621
2010 Zebrafish Git2a is required for cell movements during gastrulation; its depletion arrests directed cell migration toward the vegetal pole and reduces cell contractility. Git2a regulates phosphorylation of myosin light chain (MLC), thereby controlling myosin II-mediated cell contractility. The phenotype is rescued by chicken GIT2, confirming functional conservation. Antisense morpholino knockdown; time-lapse microscopy; myosin light chain phosphorylation assay; pharmacological inhibition with Blebbistatin; rescue with chicken GIT2 Developmental biology High 21034731
2013 PKL/GIT2 regulates activity of the Rac1 GEF Vav2 through a phosphorylation-dependent interaction. PKL is required for Vav2 activation downstream of integrin engagement and EGF stimulation. Vav2 in turn regulates redistribution of PKL and β-PIX to focal adhesions after EGF stimulation, forming a feedforward signaling loop. Vav2 knockdown reduces directional persistence and polarization of migrating cells. Co-immunoprecipitation; PKL and Vav2 knockdown; Rac1 activation assays; immunofluorescence localization of PKL and β-PIX; cell migration directionality assays Molecular biology of the cell High 23615439
2013 Loss of Git2 promotes epithelial-mesenchymal transition (EMT) through a pathway involving enhanced maturation of miR-146a, which suppresses Cnot6L (a deadenylase), leading to stabilization of Zeb1 mRNA and increased Zeb1 expression. Git2 knockdown/knockout; miR-146a maturation assay; Cnot6L manipulation; Zeb1 mRNA stability assay; EMT marker analysis Journal of cell science Medium 23591815
2014 GIT2 negatively regulates TLR-induced NF-κB and MAPK signaling by recruiting the deubiquitinating enzyme Cylindromatosis (CYLD) to inhibit K63-linked ubiquitination of TRAF6, thereby terminating downstream inflammatory signaling. Git2-deficient mice and macrophages show dramatically increased pro-inflammatory cytokine production in response to TLR stimulation. Git2-knockout mice and macrophages; TLR stimulation assays; NF-κB and MAPK activation measurements; Co-immunoprecipitation of GIT2-CYLD complex; TRAF6 ubiquitination assay Proceedings of the National Academy of Sciences of the United States of America High 24879442
2015 GIT2 localizes to the nucleus, is phosphorylated by ATM kinase following DNA damage, and forms complexes with multiple DNA damage response (DDR) factors. GIT2 targeting to DNA double-strand breaks depends on H2AX, ATM, and MRE11 but is independent of MDC1 and RNF8. GIT2 promotes DNA repair by stabilizing BRCA1 in repair complexes, upregulating HMGN1 and RFC1, and regulating PARP activity. GIT2-knockout mice show increased susceptibility to irradiation-induced DNA damage. Nuclear fractionation; Co-immunoprecipitation with DDR factors; ATM kinase phosphorylation assay; DDR factor dependency analysis (H2AX/ATM/MRE11/MDC1/RNF8); GIT2-KO mice irradiation; PARP activity assay; immunofluorescence foci analysis Molecular and cellular biology High 25605334
2016 GIT2 restricts focal adhesion recruitment of DOCK5 and inhibits DOCK5 interaction with Crk, thereby suppressing DOCK5-dependent activation of the Crk-p130Cas signaling cascade, Rac1-mediated lamellipodial protrusion, and FA turnover. GIT2 is recruited to focal adhesions in response to Rho-ROCK signaling and actomyosin contractility. GIT2 knockdown/overexpression; Co-immunoprecipitation of GIT2-DOCK5-Crk interactions; ROCK and MLC inhibition; Rac1 activation assay; invasion assays in epithelial cells Oncogene High 27669437
2016 RUSC2 interacts with the Spa Homology Domain (SHD) of GIT2 in lung cancer cells, stabilizes GIT2 by decreasing its degradation and increasing its phosphorylation, and promotes Golgi reorientation and directional migration. EGF stimulation transiently increases RUSC2-GIT2 interaction, while prolonged EGF stimulation decreases it via Rab35 activation. Rab35 silencing reduces GIT2 stability and phosphorylation. Co-immunoprecipitation (RUSC2-GIT2 interaction); RUSC2 and Rab35 silencing; GIT2 stability assays; Golgi reorientation assay; directional migration assay Cancer letters Medium 27238570
2016 GIT2 physically interacts with the insulin receptor and insulin receptor substrate 2 (IRS-2) in pancreatic tissue; this interaction is diminished in diabetic db/db mice. Genomic deletion of GIT2 disrupts pancreatic beta cell mass and reduces insulin secretion, leading to elevated plasma glucose and insulin resistance. Co-immunoprecipitation of GIT2 with insulin receptor and IRS-2; GIT2-KO mouse metabolic phenotyping; pancreatic islet transcriptomics Frontiers in endocrinology Medium 26834700
2018 GIT2/PKL mediates endothelial progenitor cell (EPC) migration downstream of CXCR2 via the Src-PKL/Vav2-Rac1 signaling pathway. Phosphorylation and co-localization of PKL and Vav2 are required for Rac1 activation and development of lamellipodia/filopodia driving EPC migration. Transwell migration assays; shRNA knockdown; signaling inhibitors; immunofluorescence co-localization of PKL and Vav2; Rac1 phosphorylation assays FASEB journal Medium 29229683
2024 GIT2 associates with centrosomes and γ-tubulin complex proteins in mast cells. Depletion of GIT2 enhances centrosomal microtubule nucleation. Phosphorylation of GIT2 by conventional protein kinase C (PKC) promotes its centrosomal localization and microtubule nucleation during FcεRI-induced activation. GIT2 (unlike GIT1) acts as a negative regulator of microtubule nucleation in mast cells and also participates in antigen-induced degranulation and chemotaxis. shRNA depletion; immunofluorescence and Co-IP with γ-tubulin complex proteins; time-lapse microtubule nucleation assay; PKC inhibitor treatment; site-directed mutagenesis of phosphorylation sites; phenotypic rescue Frontiers in immunology High 38370406
2025 GIT2 directly binds NF-κB components p65 (canonical) and p52 (non-canonical) to inhibit their activation, and positively regulates TRAF3 expression to further suppress both canonical and non-canonical NF-κB signaling. GIT2 thereby promotes osteogenic differentiation of bone marrow mesenchymal stem cells (BMSCs) and alleviates DNA damage-induced cellular senescence. Co-immunoprecipitation (GIT2 with p65 and p52); Western blotting of NF-κB pathway components; GIT2 overexpression/knockdown in BMSCs; comet assay; in vivo ovariectomy mouse model; micro-CT bone analysis Tissue & cell Medium 39954559
2025 THRAP3 recruits the splicing factor SLU7 to facilitate skipping of GIT2 Exon14, generating a GIT2 splice variant that promotes ferroptosis resistance in AML cells by inhibiting iron accumulation and promoting GSH synthesis. Inhibition of GIT2 Exon14 skipping reverses THRAP3-induced ferroptosis resistance in vitro and in vivo. THRAP3 knockdown/overexpression; Co-immunoprecipitation of THRAP3-SLU7; RT-PCR/splicing assays for Exon14; ferroptosis assays (RSL3/erastin); iron and GSH measurement; orthotopic mouse models Nature communications Medium 41326370
2025 In glioblastoma cells, GIT2 associates with γ-tubulin ring complex (γTuRC) proteins and localizes to centrosomes. Depletion of GIT2 enhances centrosomal microtubule nucleation. The N-terminal ArfGAP domain of GIT2 is responsible for centrosomal localization and regulation of microtubule nucleation. PKC phosphorylates GIT2 at serine 46 (S46) on the ArfGAP domain, and phosphomimetic S46 promotes microtubule nucleation. shRNA depletion; immunofluorescence; time-lapse microtubule nucleation; immunoprecipitation with γTuRC components; site-directed mutagenesis (S46); kinase assay with PKC inhibitors Cancer cell international High 40176062

Source papers

Stage 0 corpus · 42 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). The Journal of cell biology 144 11448998
2000 The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing. The Journal of biological chemistry 118 10896954
2001 A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT. The EMBO journal 86 11157752
2003 Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts. Molecular biology of the cell 76 12857867
2001 An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization. Molecular biology of the cell 75 11251077
2006 GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover. The EMBO journal 65 16628223
2006 Neutrophil direction sensing and superoxide production linked by the GTPase-activating protein GIT2. Nature immunology 64 16715100
1988 The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21. Cytogenetics and cell genetics 50 3378452
2018 Mesenchymal stem cells promote endothelial progenitor cell migration, vascularization, and bone repair in tissue-engineered constructs via activating CXCR2-Src-PKL/Vav2-Rac1. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 43 29229683
2007 Differential expression of the ARF GAP genes GIT1 and GIT2 in mouse tissues. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 40 17565117
2017 The developmental regulator PKL is required to maintain correct DNA methylation patterns at RNA-directed DNA methylation loci. Genome biology 39 28569170
2012 GIT2 acts as a potential keystone protein in functional hypothalamic networks associated with age-related phenotypic changes in rats. PloS one 38 22606319
2010 Regulation of thymocyte positive selection and motility by GIT2. Nature immunology 38 20431621
2014 The GTPase-activating protein GIT2 protects against colitis by negatively regulating Toll-like receptor signaling. Proceedings of the National Academy of Sciences of the United States of America 33 24879442
2016 The focal adhesion-associated proteins DOCK5 and GIT2 comprise a rheostat in control of epithelial invasion. Oncogene 30 27669437
2015 Nuclear GIT2 is an ATM substrate and promotes DNA repair. Molecular and cellular biology 30 25605334
2016 GIT2 Acts as a Systems-Level Coordinator of Neurometabolic Activity and Pathophysiological Aging. Frontiers in endocrinology 29 26834700
2017 A novel GIT2-BRAF fusion in pilocytic astrocytoma. Diagnostic pathology 28 29141672
2016 EGF-stimulated activation of Rab35 regulates RUSC2-GIT2 complex formation to stabilize GIT2 during directional lung cancer cell migration. Cancer letters 26 27238570
2018 GIT2-A keystone in ageing and age-related disease. Ageing research reviews 25 29452267
2008 Anxiety-like behaviors in mice lacking GIT2. Neuroscience letters 22 19114090
2012 The cytoskeletal regulatory scaffold protein GIT2 modulates mesenchymal stem cell differentiation and osteoblastogenesis. Biochemical and biophysical research communications 21 22846567
2017 Genomic deletion of GIT2 induces a premature age-related thymic dysfunction and systemic immune system disruption. Aging 19 28260693
2020 Long non-coding RNA MALAT1 promotes odontogenic differentiation of human dental pulp stem cells by impairing microRNA-140-5p-dependent downregulation of GIT2. Cell and tissue research 18 32743695
1990 Assignment of the rat genes coding for phenylalanine hydroxylase (PAH), tyrosine aminotransferase (TAT), and pyruvate kinase (PKL) to chromosomes 7, 19, 2, respectively. Cytogenetics and cell genetics 18 1973378
2013 Loss of Git2 induces epithelial-mesenchymal transition by miR146a-Cnot6L-controlled expression of Zeb1. Journal of cell science 15 23591815
2010 Emerging role of paxillin-PKL in regulation of cell adhesion, polarity and migration. Cell adhesion & migration 14 20372092
2013 Paxillin kinase linker (PKL) regulates Vav2 signaling during cell spreading and migration. Molecular biology of the cell 10 23615439
2010 The cell adhesion-associated protein Git2 regulates morphogenetic movements during zebrafish embryonic development. Developmental biology 10 21034731
2021 Physiological and genomic evidence supports the role of Serratia quinivorans PKL:12 as a biopriming agent for the biohardening of micropropagated Picrorhiza kurroa plantlets in cold regions. Genomics 8 33744342
2017 Genetic deletion of GIT2 prolongs functional recovery and suppresses chondrocyte differentiation in rats with rheumatoid arthritis. Journal of cellular biochemistry 8 28777475
2024 Git2 deficiency promotes MDSCs recruitment in intestine via NF-κB-CXCL1/CXCL12 pathway and ameliorates necrotizing enterocolitis. Mucosal immunology 6 39074614
2015 GIT2 deficiency attenuates concanavalin A-induced hepatitis in mice. FEBS open bio 6 26380813
2019 GIT2 deficiency attenuates inflammation-induced expression of pro-labor mediators in human amnion and myometrial cells†. Biology of reproduction 3 30915469
2016 [Effect of GTPase activating protein Git2 on metastasis in breast cancer]. Zhonghua zhong liu za zhi [Chinese journal of oncology] 2 27531261
2008 Expression analysis of a novel pyridoxal kinase messenger RNA splice variant, PKL, in oil rape suffering abiotic stress and phytohormones. Acta biochimica et biophysica Sinica 2 19089298
2025 GIT2 negatively regulates the NF-κB pathway directly or indirectly by regulating TRAF3 expression to promote osteogenic differentiation of BMSCs. Tissue & cell 1 39954559
2024 Regulation of microtubule nucleation in mouse bone marrow-derived mast cells by ARF GTPase-activating protein GIT2. Frontiers in immunology 1 38370406
2025 Regulation of microtubule nucleation in glioblastoma cells by ARF GTPase-activating proteins GIT1 and GIT2 and protein kinase C. Cancer cell international 0 40176062
2025 THRAP3 promotes ferroptosis resistance in acute myelocytic leukemia through SLU7-mediated alternative splicing of GIT2. Nature communications 0 41326370
2025 PKL mediates H3K4me2 modification and spatial gene congregation in chromatin regulation. Nucleic acids research 0 41359383
2017 [High-Content siRNA Screen of the Kinome Identifies Kinases Involved in Git2-Induced Mesenchymal-Epithelial Transition]. Molekuliarnaia biologiia 0 28900089

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