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Showing ARHGAP17 — RICH1 is a alias.

ARHGAP17

Rho GTPase-activating protein 17 · UniProt Q68EM7

Length
881 aa
Mass
95.4 kDa
Annotated
2026-06-09
22 papers in source corpus 19 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

ARHGAP17 (RICH1/NADRIN) is a BAR-domain–containing RhoGAP that inactivates the Rho-family GTPases Cdc42, Rac1, and RhoA to control actin cytoskeletal remodeling, epithelial junction integrity, and downstream proliferative and morphogenetic signaling (PMID:10967100, PMID:26004135). Its N-terminal BAR domain binds and tubulates membrane lipids, directing GAP activity to the plasma membrane and supporting oligomerization (PMID:15240152, PMID:22975681), and its GAP activity is required for its cellular effects on actin organization, neurite outgrowth, astrocyte stellation, and exocytosis (PMID:10967100, PMID:15240152, PMID:23355722). At epithelial tight junctions ARHGAP17 is recruited by the scaffold angiomotin (Amot) into a Pals1/Patj/Par-3 complex where it locally regulates Cdc42 to maintain junction integrity, a role confirmed in vivo by intestinal barrier defects in knockout mice (PMID:16678097, PMID:27229483). At invadopodia it is spatiotemporally repositioned from the ring to the core via its Cdc42 effector partner CIP4, restricting Cdc42 activity to drive structure disassembly (PMID:36571786). Through its BAR domain it competes with Merlin for Amot-p80 binding to activate the Hippo kinase cascade and restrain stemness (PMID:35064101), and it links the NME1–CDC42–cytoskeleton axis to Hippo/YAP regulation (PMID:41978798). ARHGAP17 activity is tuned by PKA/PKG phosphorylation at Ser-702, which disrupts CIP4 binding (PMID:26507661), by Src-family tyrosine phosphorylation that switches its isoform-specific GTPase targeting (PMID:24703939), and by CUL4-Wdr4–mediated ubiquitination and degradation (PMID:36681682); it also scaffolds TRIM21-dependent ubiquitination of RhoA (PMID:41436617). Across cancer models ARHGAP17 acts as a growth- and invasion-suppressing GAP upstream of Rac1/Cdc42-PAK1-ERK and Wnt/β-catenin signaling (PMID:26004135, PMID:29730655, PMID:35293764).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 2000 High

    Established that ARHGAP17/NADRIN is a functional RhoGAP whose catalytic activity drives actin remodeling and regulated exocytosis, defining its core molecular identity.

    Evidence In vitro GAP assay against RhoA/Rac1/Cdc42 plus domain-deletion mutants in NIH3T3 and PC12 cells with exocytosis readout

    PMID:10967100

    Open questions at the time
    • GTPase target specificity in vivo not resolved
    • structural basis of GAP activity not defined
  2. 2002 Medium

    Showed that alternative splicing produces functionally distinct isoforms with isoform-specific effects on neurite outgrowth and nuclear translocation of a C-terminal fragment, indicating isoform-encoded functional diversity.

    Evidence Splice variant identification with GAP-mutant neurite outgrowth assays and subcellular fractionation in PC12 cells

    PMID:12358749

    Open questions at the time
    • function of the nuclear C-terminal fragment unknown
    • single-lab isoform characterization
  3. 2004 Medium

    Demonstrated that the BAR domain binds and deforms membranes and mediates oligomerization, providing the structural basis for membrane targeting of the GAP.

    Evidence Liposome tubulation, lipid-binding, and BS3 crosslinking assays in vitro

    PMID:15240152

    Open questions at the time
    • lipid species preference not mapped
    • in-cell consequences of tubulation untested
  4. 2006 High

    Identified the Amot scaffold as the recruiter of ARHGAP17 to a tight junction complex, explaining how Cdc42 regulation is spatially restricted to maintain epithelial junctions.

    Evidence Proteomic screen, Co-IP, domain mapping, and tight junction maintenance assays in MDCK cells

    PMID:16678097

    Open questions at the time
    • mechanism of GAP activation within the complex unknown
    • direct vs indirect Amot binding not fully resolved
  5. 2012 Medium

    Established that distinct isoforms selectively target RhoA, Cdc42, or Rac1 and that the BAR domain controls both membrane localization and GAP activity in platelets, linking isoform identity to GTPase choice.

    Evidence Isoform-specific overexpression, GTPase activity assays, BAR deletion, and fibrinogen adhesion assays in platelets

    PMID:22975681

    Open questions at the time
    • determinants of isoform-specific GTPase selectivity unclear
    • single-lab characterization
  6. 2013 Medium

    Showed that signal-induced conformational change releases an autoinhibitory dimer and routes ARHGAP17 to ERM/EBP50 complexes to inactivate RhoA during astrocyte stellation, revealing a regulated activation switch.

    Evidence Co-IP, domain-deletion analysis, GAP-mutant rescue, and stellation assays in cultured astrocytes

    PMID:23355722

    Open questions at the time
    • structural basis of intramolecular dimer not defined
    • signal-to-conformation coupling not mechanistically resolved
  7. 2015 High

    Defined PKA/PKG phosphorylation at Ser-702 as a regulatory switch that disrupts CIP4 binding and enhances Rac1-specific inhibition of migration, connecting cyclic-nucleotide signaling to GAP function.

    Evidence Phos-tag site mapping, ARHGAP17-CIP4 Co-IP, Rac1-GTP pulldown, and migration assays in platelets

    PMID:26507661

    Open questions at the time
    • how CIP4 binding gates GAP activity not fully mechanistic
    • Ser-702 role outside platelets untested
  8. 2015 Medium

    Placed ARHGAP17 upstream of a CDC42/RAC1-PAK1-ERK1/2 axis controlling proliferation and adhesion, linking its GAP activity to mitogenic signaling output.

    Evidence Overexpression/knockdown, GTPase activity assays, phospho-Western, and cell cycle/adhesion assays in HL7702 hepatocytes

    PMID:26004135

    Open questions at the time
    • direct vs indirect effect on PAK1/ERK not separated
    • single cell line
  9. 2014 Medium

    Revealed that Src-family tyrosine phosphorylation switches isoform-specific GTPase targeting, adding a kinase-controlled layer to ARHGAP17 output during platelet activation.

    Evidence Platelet activation, kinase Co-IP, Src-family inhibitor phosphorylation assays, and isoform-specific GTPase activity assays

    PMID:24703939

    Open questions at the time
    • phosphosite identities not mapped
    • mechanism converting RhoGAP to GTPase-activating output unclear
  10. 2016 High

    Provided in vivo proof that ARHGAP17 maintains intestinal epithelial barrier integrity through proper apical junction localization, validating the cell-based tight junction model.

    Evidence Arhgap17 knockout mouse with paracellular permeability and junction immunofluorescence

    PMID:27229483

    Open questions at the time
    • GTPase responsible for the in vivo phenotype not pinned down
    • tissue-specific contribution not dissected
  11. 2018 Medium

    Positioned ARHGAP17 as a tumor-suppressing GAP downstream of VEGF/NRP1 and upstream of Wnt/β-catenin, connecting its Cdc42/Rac1 control to cancer cell migration and metastasis.

    Evidence VEGF KO/soluble NRP1, expression profiling, Cdc42 activity and filopodia imaging; plus overexpression/knockdown, in vivo metastasis, and WIF-1 epistasis in colon cancer

    PMID:29730655 PMID:29971782

    Open questions at the time
    • mechanistic link from GAP activity to β-catenin/GSK3β not direct
    • single-lab models
  12. 2022 High

    Established spatiotemporal control of Cdc42 at invadopodia, showing CIP4-mediated ring-to-core translocation of ARHGAP17 drives structure disassembly, a high-resolution mechanistic picture of its GAP function.

    Evidence Live imaging, Cdc42 FRET biosensor, knockdown, and CIP4 Co-IP at invadopodia

    PMID:36571786

    Open questions at the time
    • upstream signal triggering translocation unknown
    • general applicability beyond invadopodia untested
  13. 2022 Medium

    Defined a BAR-domain-dependent competition with Merlin for Amot-p80 that activates the Hippo cascade and restrains stemness, linking ARHGAP17 to Hippo regulation in addition to GTPase control.

    Evidence Co-IP of RICH1-Amot-p80-Merlin, BAR deletion, MST/LATS activity, and stemness assays in breast cancer cells

    PMID:35064101

    Open questions at the time
    • whether Hippo effect is GAP-independent not fully resolved
    • single-lab study
  14. 2022 Medium

    Confirmed ARHGAP17 acts upstream of Rac1 to control apoptosis and chemoresistance, reinforcing its GAP-dependent role in cancer cell survival across stress contexts.

    Evidence Rac1-GTP pulldown, pharmacological epistasis, apoptosis markers, and xenograft in colon cancer; cyclic-strain apoptosis model in periodontal fibroblasts

    PMID:32391922 PMID:35293764

    Open questions at the time
    • downstream apoptotic effectors of Rac1 not specified
    • single-lab models
  15. 2023 High

    Identified CUL4-Wdr4–mediated ubiquitination and degradation as a mechanism controlling ARHGAP17 abundance, thereby gating Rac1 activity and neural progenitor proliferation in vivo.

    Evidence Wdr4 mouse KO, ubiquitination assay, Rac1-GTP pulldown, and cerebellar histology

    PMID:36681682

    Open questions at the time
    • ubiquitination sites on ARHGAP17 not mapped
    • signals regulating Wdr4-ARHGAP17 axis unknown
  16. 2025 Medium

    Showed ARHGAP17 scaffolds TRIM21-dependent ubiquitination of RhoA, coupling GTPase degradation to STAT3 suppression and M1 macrophage polarization, extending its function into immune regulation.

    Evidence Co-IP of RICH1-TRIM21-RhoA, ubiquitination assay, STAT3 phospho-Western, cytokine and macrophage polarization assays in breast cancer

    PMID:41436617

    Open questions at the time
    • whether scaffolding is GAP-activity-dependent unclear
    • single-lab study
  17. 2026 Medium

    Connected NME1 histidine-phosphorylation to ARHGAP17-CDC42 control of the cytoskeleton and Hippo/YAP signaling, placing ARHGAP17 within an upstream metabolic-kinase input.

    Evidence PhastID proximity labeling, CDC42 activity assay, and YAP phosphorylation/localization with NME1 loss-of-function

    PMID:41978798

    Open questions at the time
    • direct NME1-ARHGAP17 interaction vs proximity not distinguished
    • single study

Open questions

Synthesis pass · forward-looking unresolved questions
  • How isoform identity, post-translational modification, scaffold binding, and degradation are integrated to determine which GTPase ARHGAP17 acts on in a given cell remains unresolved.
  • no unified structural model of GTPase selectivity
  • interplay of Ser-702, Tyr phosphorylation, and ubiquitination not co-analyzed
  • in vivo isoform-specific functions largely untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3 GO:0008289 lipid binding 2 GO:0140096 catalytic activity, acting on a protein 1
Localization
GO:0005856 cytoskeleton 2 GO:0005886 plasma membrane 2 GO:0005634 nucleus 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1500931 Cell-Cell communication 2 R-HSA-5357801 Programmed Cell Death 2
Partners
AMOTCIP4EBP50NME1TRIM21
Complex memberships
Amot tight junction complex (Pals1/Patj/Par-3)

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 NADRIN (ARHGAP17) contains a GAP domain that activates RhoA, Rac1, and Cdc42 GTPases in vitro. Expression in NIH3T3 cells reduced actin stress fibers and ruffled membranes. In PC12 cells, NADRIN co-localized with synaptotagmin at neurite termini and with cortical actin filaments. Expression of NADRIN or its coiled-coil+GAP domain mutant enhanced Ca2+-dependent exocytosis, while a GAP-domain-lacking mutant inhibited exocytosis, establishing that GAP activity is required for its role in regulated exocytosis. In vitro GAP assay, NIH3T3 cell morphology, PC12 cell co-localization and exocytosis assay with domain-deletion mutants The Journal of biological chemistry High 10967100
2002 Three novel splice variants of NADRIN (ARHGAP17) were identified (nadrin-102, -104, -116, -126). Nadrin-116 inhibited NGF-dependent neurite outgrowth in a GAP-activity-dependent manner, while other variants had no effect. The 66-kDa C-terminal fragment of nadrin-102 and nadrin-116 localized to the nucleus, and NGF-induced differentiation accelerated this nuclear translocation. Splice variant identification, PC12 cell neurite outgrowth assay with GAP-mutants, subcellular fractionation and localization Journal of neurochemistry Medium 12358749
2004 The BAR domain of RICH-1 (ARHGAP17) binds membrane lipids and deforms spherical liposomes into striated tubes, consistent with oligomerization via a coiled-coil region within the BAR domain. RICH-1 forms oligomers in the presence of the chemical cross-linker BS3. Liposome tubulation assay, lipid-binding assay, chemical crosslinking (BS3) Biochemical and biophysical research communications Medium 15240152
2006 RICH1 (ARHGAP17) binds the scaffolding protein angiomotin (Amot), which targets RICH1 to a tight junction complex containing Pals1, Patj, and Par-3. Regulation of Cdc42 by RICH1 is necessary for maintenance of tight junctions in MDCK epithelial cells. The coiled-coil domain of Amot, required for Rich1 binding, is also necessary for Amot localization to apical membranes and for Amot to relocalize Pals1 and Par-3 to internal puncta. Proteomic screen (functional and protein interaction), Co-IP, MDCK cell tight junction assays, domain-deletion experiments Cell High 16678097
2012 Nadrin (ARHGAP17) is present in platelets where it co-localizes with actin-rich regions and Rho GTPases. Different Nadrin isoforms selectively regulate RhoA, Cdc42, or Rac1. The BAR domain controls Nadrin-GAP activity and directs the GAP to the plasma membrane. Nadrin overexpression strongly reduced platelet cell adhesion on fibrinogen and controls RhoA-mediated stress fiber and focal adhesion formation. Isoform-specific overexpression, Rho GTPase activity assays, co-localization, spreading/adhesion assay on fibrinogen, BAR domain deletion Cellular signalling Medium 22975681
2013 NADRIN (ARHGAP17) expression increased in stellate astrocytes. Induced expression accelerated morphological differentiation of cultured astrocytes into stellate cells in a GAP-activity-dependent manner. NADRIN formed a dimer via amino- and carboxy-terminal domain interaction, which was disrupted by inductive signals (dibutyryl-cAMP, EGF). Upon inductive signals, NADRIN formed a complex with ERM proteins via ERM-binding phosphoprotein 50 (EBP50) through its C-terminal PDZ-binding motif, where it inactivates RhoA. Immunoprecipitation (co-IP), GAP-activity mutant rescue, astrocyte stellation assay, domain-deletion analysis Journal of biochemistry Medium 23355722
2014 Nadrin (ARHGAP17) becomes tyrosine-phosphorylated upon platelet activation by Src family kinases (Src, Lyn, Fyn). Phosphorylation leads to isoform- and target-specific regulation: Src-phosphorylation of Nadrin5 mediates Cdc42 inactivation, while Src-phosphorylation of Nadrin2 leads to RhoA and Rac1 activation. Platelet activation assay, kinase co-IP, phosphorylation assays with Src-family inhibitors, isoform-specific Rho GTPase activity assays Cellular signalling Medium 24703939
2015 PKA and PKG phosphorylate ARHGAP17 at serine 702 in platelets, which is mapped using Phos-tag gels. ARHGAP17 binds CIP4 in platelets and Ser-702 phosphorylation interferes with CIP4 binding; reduced CIP4 binding results in enhanced inhibition of cell migration by ARHGAP17. PKA/PKG activation reduces Rac1-GTP levels, and ARHGAP17 is identified as a Rac1-specific GAP mediating this effect. Phos-tag gel phosphorylation mapping, Co-IP/pulldown of ARHGAP17-CIP4 complex, Rac1-GTP assay (pull-down), cell migration assay The Journal of biological chemistry High 26507661
2015 Rich1 (ARHGAP17) overexpression in hepatocyte HL7702 epithelial cells causes S-phase arrest, proliferation inhibition, and adhesion decline with decreased F-actin. Rich1 stimulates GTP hydrolysis on both CDC42 and RAC1, attenuating their activity and the phosphorylation of PAK1 and ERK1/2. GAP-domain-deleted Rich1 or Rich1 silencing abolished all these effects, establishing a CDC42/RAC1-PAK1-ERK1/2 signaling axis. Overexpression/knockdown, Rho GTPase activity assay (GTP hydrolysis), phosphorylation (Western blot), cell cycle analysis, adhesion assay Cellular signalling Medium 26004135
2016 Arhgap17-deficient mice show increased paracellular permeability and aberrant localization of the apical junction complex in intestinal luminal epithelium, establishing a role for Arhgap17 in regulating transcellular transport and maintaining intestinal barrier integrity in vivo. Knockout mouse model, paracellular permeability assay, immunofluorescence localization of apical junction complex Scientific reports High 27229483
2018 VEGF long isoform acting through NRP1 controls filopodia formation and cell migration of breast cancer cells by modulating Cdc42 activity via ARHGAP17. Genome-wide expression profiling identified ARHGAP17 as a target gene downstream of the VEGF/NRP1 signal, and VEGF knockout or soluble NRP1 overexpression impaired cell migration concordantly with altered ARHGAP17 expression and Cdc42 activity. VEGF knockout, soluble NRP1 overexpression, genome-wide expression profiling, Cdc42 activity assay, filopodia imaging International journal of cancer Medium 29971782
2018 ARHGAP17 overexpression in colon cancer cells inhibits cell growth and invasion and restricts lung metastasis in vivo. Mechanistically, ARHGAP17 increases phosphorylation of GSK3β and decreases β-catenin nuclear localization and transcriptional activity. WIF-1-mediated inhibition of Wnt signaling attenuated the proliferation/invasion promotion caused by ARHGAP17 knockdown, placing ARHGAP17 upstream of Wnt/β-catenin. Overexpression/knockdown, in vivo metastasis model, Western blot for β-catenin/GSK3β phosphorylation, GSEA, Wnt inhibitor epistasis Cellular physiology and biochemistry Medium 29730655
2020 ARHGAP17 overexpression abolished pathological cyclic strain-induced apoptosis in human periodontal ligament fibroblasts by inactivating Rac1/Cdc42. Rac1 inhibitors (NSC23766, EHT 1864) attenuated ARHGAP17 knockdown-mediated apoptosis, confirming epistatic placement of ARHGAP17 upstream of Rac1/Cdc42 in the apoptosis pathway. Cyclic strain model, overexpression/knockdown, Rac1/Cdc42 activity assay, pharmacological inhibition epistasis, apoptosis assay Clinical and experimental pharmacology & physiology Medium 32391922
2022 ARHGAP17 is a Cdc42-specific RhoGAP that localizes to the invadopodia ring during assembly, restricting Cdc42 activity to the invadopodia core. During disassembly, ARHGAP17 translocates from the ring to the core in a process mediated by its interaction with the Cdc42 effector CIP4. Once at the core, ARHGAP17 inactivates Cdc42 to promote invadopodia disassembly, defining a spatiotemporal regulatory mechanism for Cdc42 at invadopodia. Live imaging, FRAP/localization at invadopodia, Cdc42 activity biosensor (FRET-based), knockdown, Co-IP with CIP4 The Journal of cell biology High 36571786
2022 RICH1 (ARHGAP17) activates the Hippo kinase cascade in breast cancer cells by competing with Merlin for binding to Amot-p80. This competition is mediated by the BAR domain of RICH1; deletion of the BAR domain abolished RICH1's ability to displace Amot-p80 from Merlin. Loss of RICH1 promoted stemness and disrupted epithelial architecture. Co-IP (RICH1-Amot-p80-Merlin complex), BAR domain deletion mutant, Hippo pathway kinase activity (MST1/2, LATS), stemness assays Cell death & disease Medium 35064101
2022 ARHGAP17 knockdown in colon cancer cells led to elevated active Rac1 levels, while ARHGAP17 overexpression reduced active Rac1 and sensitized 5-FU-resistant cells to apoptosis. Rac1 inhibitor abolished the anti-apoptotic effect of ARHGAP17 knockdown, and Rac1 overexpression reversed the pro-apoptotic effect of ARHGAP17 overexpression, placing ARHGAP17 upstream of Rac1 in the apoptosis pathway. Rac1-GTP pull-down assay, overexpression/knockdown, pharmacological Rac1 inhibition epistasis, apoptosis (cleaved caspase-3, PARP), in vivo xenograft Neoplasma Medium 35293764
2023 Wdr4, a substrate adaptor of the CUL4 E3 ligase complex, induces ubiquitination and degradation of Arhgap17 in cerebellar granule neuron progenitors (GNPs), thereby activating Rac1 and facilitating cell cycle progression. Loss of Wdr4 in GNPs increased Arhgap17 levels, reduced Rac1 activity, and caused proliferation defects and cerebellar developmental abnormalities. Genetic mouse KO, ubiquitination assay, Rac1-GTP pull-down, cell cycle analysis, cerebellar immunohistology Cell death & disease High 36681682
2025 RICH1 (ARHGAP17) facilitates ubiquitination-mediated degradation of RhoA by binding TRIM21 E3 ligase and enhancing TRIM21-RhoA interaction in breast cancer cells. This leads to decreased STAT3 phosphorylation, increased IFN-γ production/secretion, and promotion of M1-like macrophage polarization. Co-IP (RICH1-TRIM21-RhoA complex), ubiquitination assay, STAT3 phosphorylation Western blot, cytokine secretion assay, macrophage polarization assay NPJ precision oncology Medium 41436617
2026 NME1, whose histidine phosphorylation is required for its activity, modulates CDC42 activity via ARHGAP17, thereby influencing cytoskeletal organization and Hippo pathway activation. Loss of NME1 reduced YAP phosphorylation and promoted YAP nuclear localization, consistent with suppression of Hippo signaling through the NME1-ARHGAP17-CDC42-cytoskeleton axis. Identified using PhastID-based proximity labeling. PhastID proximity labeling, CDC42 activity assay, YAP phosphorylation/localization assay, loss-of-function Life medicine Medium 41978798

Source papers

Stage 0 corpus · 22 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells. Cell 303 16678097
2000 Nadrin, a novel neuron-specific GTPase-activating protein involved in regulated exocytosis. The Journal of biological chemistry 56 10967100
2004 RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes. Biochemical and biophysical research communications 40 15240152
2019 ARHGAP17 suppresses tumor progression and up-regulates P21 and P27 expression via inhibiting PI3K/AKT signaling pathway in cervical cancer. Gene 28 30641218
2015 Cyclic Nucleotide-dependent Protein Kinases Target ARHGAP17 and ARHGEF6 Complexes in Platelets. The Journal of biological chemistry 28 26507661
2018 Long isoform of VEGF stimulates cell migration of breast cancer by filopodia formation via NRP1/ARHGAP17/Cdc42 regulatory network. International journal of cancer 25 29971782
2016 Arhgap17, a RhoGTPase activating protein, regulates mucosal and epithelial barrier function in the mouse colon. Scientific reports 23 27229483
2012 Isoform-specific roles of the GTPase activating protein Nadrin in cytoskeletal reorganization of platelets. Cellular signalling 21 22975681
2002 Identification and functional characterization of nadrin variants, a novel family of GTPase activating protein for rho GTPases. Journal of neurochemistry 21 12358749
2015 Rich1 negatively regulates the epithelial cell cycle, proliferation and adhesion by CDC42/RAC1-PAK1-Erk1/2 pathway. Cellular signalling 19 26004135
2018 Tumor Suppressive Role of ARHGAP17 in Colon Cancer Through Wnt/β-Catenin Signaling. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 17 29730655
2022 RICH1 inhibits breast cancer stem cell traits through activating kinases cascade of Hippo signaling by competing with Merlin for binding to Amot-p80. Cell death & disease 16 35064101
2022 ARHGAP17 regulates the spatiotemporal activity of Cdc42 at invadopodia. The Journal of cell biology 11 36571786
2020 ARHGAP17 inhibits pathological cyclic strain-induced apoptosis in human periodontal ligament fibroblasts via Rac1/Cdc42. Clinical and experimental pharmacology & physiology 11 32391922
2013 The role of NADRIN, a Rho GTPase-activating protein, in the morphological differentiation of astrocytes. Journal of biochemistry 11 23355722
2023 Wdr4 promotes cerebellar development and locomotion through Arhgap17-mediated Rac1 activation. Cell death & disease 10 36681682
2014 Nadrin GAP activity is isoform- and target-specific regulated by tyrosine phosphorylation. Cellular signalling 10 24703939
2022 ARHGAP17 enhances 5-Fluorouracil-induced apoptosis in colon cancer cells by suppressing Rac1. Neoplasma 3 35293764
2024 ARHGAP17 Inhibits Hepatocellular Carcinoma Progression by Inactivation of Wnt/β-Catenin Signaling Pathway. Biochemical genetics 1 38724713
2026 Histidine phosphorylation of NME1 regulates the Hippo pathway via the ARHGAP17-CDC42-cytoskeleton axis. Life medicine 0 41978798
2025 RICH1 enhances pro-inflammatory TAM infiltration in breast cancer via promoting TRIM21-mediated ubiquitination of RhoA and inhibiting STAT3 phosphorylation. NPJ precision oncology 0 41436617
2024 RICH1 is a novel key suppressor of isoproterenol‑ or angiotensin II‑induced cardiomyocyte hypertrophy. Molecular medicine reports 0 38456539

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