Affinage

RHOU

Rho-related GTP-binding protein RhoU · UniProt Q7L0Q8

Length
258 aa
Mass
28.2 kDa
Annotated
2026-06-10
31 papers in source corpus 23 papers cited in narrative 23 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

RHOU (Wrch-1) is an atypical Rho-family GTPase that couples non-canonical Wnt and cytokine signaling to actin-cytoskeleton remodeling, cell adhesion, and migration (PMID:11459829, PMID:19397496). Biochemically it is distinguished from Cdc42 by an extremely rapid intrinsic guanine-nucleotide exchange rate and negligible GTPase activity, leaving it constitutively GTP-bound, while its N-terminal extension autoinhibits effector engagement until relieved by SH3-adaptor binding (PMID:15556869, PMID:15350535). Membrane targeting is achieved through C-terminal palmitoylation rather than prenylation, and the conserved CCFV cysteine is required for membrane localization and transformation (PMID:16046391). Its N-terminal proline-rich (PxxP) motifs recruit the SH3 adaptors Grb2 and Nck through high-avidity multivalent binding, linking activated EGFR on endosomes to RhoU GTP loading and downstream AP-1 activity and migration (PMID:21508312, PMID:23183748). In its GTP-bound state RhoU engages effectors including PAK1/PAK4, Pyk2 and the polarity protein Par6 to control filopodium formation, focal adhesion turnover, tight-junction assembly and epithelial morphogenesis (PMID:18086875, PMID:19064640, PMID:20547754). RhoU activity is regulated post-translationally: Src phosphorylation at Y254 relocalizes it from the plasma membrane to endosomes, unloads GTP and dampens PAK activation (PMID:20547754), whereas PAK4 stabilizes RhoU against Rab40A-Cullin5-mediated ubiquitination and degradation (PMID:26598620). RhoU additionally forms C-terminal palmitoylation-dependent homo-oligomers needed for full PAK activation (PMID:38180080), and regulates fast endosomal recycling through intersectin-2 on Rab4-positive endosomes (PMID:32737221). In vivo, RhoU maintains epithelial architecture of foregut endoderm, guides neural crest and cardiac development, and restrains intestinal hyperplasia by enabling actomyosin-dependent apoptosis (PMID:21156169, PMID:21903671, PMID:24607366, PMID:30834544).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2001 Medium

    Established RHOU as a Wnt-responsive Cdc42-like GTPase, defining its place as a signaling node linking Wnt to cytoskeletal and proliferative outputs.

    Evidence PAK-1/JNK-1 activation, morphology, cell cycle, and transformation assays in mouse mammary epithelial cells

    PMID:11459829

    Open questions at the time
    • Did not resolve the unusual biochemistry distinguishing RhoU from Cdc42
    • Direct effector partners not yet mapped
  2. 2004 High

    Resolved why RhoU behaves as a constitutively active GTPase—fast intrinsic exchange with no GTPase activity—and showed the N-terminal extension autoinhibits effector binding until relieved by SH3 adaptors.

    Evidence In vitro nucleotide exchange/GTPase assays, N-terminal truncation, and co-IP with Grb2, PAK1, and NCKβ (two companion studies)

    PMID:15350535 PMID:15556869

    Open questions at the time
    • Physiological trigger for relieving N-terminal autoinhibition in vivo not defined
    • Did not address membrane targeting
  3. 2005 High

    Identified palmitoylation, not prenylation, as the membrane-anchoring modification, an atypical feature for a Rho GTPase that governs localization and transforming activity.

    Evidence Metabolic labeling, palmitoylation/prenylation inhibitors, CCFV mutagenesis, fractionation, transformation assays

    PMID:16046391

    Open questions at the time
    • Palmitoyltransferase responsible not identified
    • Dynamics of palmitoylation/depalmitoylation cycling unknown
  4. 2007 Medium

    Linked RhoU to focal adhesion turnover and migration, and identified Pyk2 as a GTP-dependent, Src-requiring effector for filopodium formation.

    Evidence Imaging, RNAi, domain mutants, migration assays, MLC phosphorylation, and Pyk2 co-IP across three studies

    PMID:17504809 PMID:17620058 PMID:18086875

    Open questions at the time
    • Quantitative hierarchy of PAK vs Pyk2 vs MLC outputs not established
    • Direct vs indirect control of MLC phosphorylation unresolved
  5. 2008 High

    Demonstrated GTP-dependent Par6 binding as the effector route by which RhoU controls tight-junction assembly and epithelial morphogenesis, and showed integrin β3 binding modulates osteoclast adhesion.

    Evidence GTP-dependent co-IP, effector-domain mutants, 3D cystogenesis, and osteoclast adhesion/migration assays

    PMID:19064640 PMID:19135548

    Open questions at the time
    • How Par6 binding integrates with the Par polarity complex downstream of RhoU not detailed
    • Structural basis of effector selection unknown
  6. 2009 Medium

    Defined the upstream transcriptional control of RhoU by non-canonical Wnt/JNK and gp130/STAT3 pathways, explaining how the constitutively active GTPase is regulated at the expression level.

    Evidence Reporter assays, promoter mapping of STAT3 sites, pathway inhibitors, and β-catenin loss-of-function

    PMID:19397496

    Open questions at the time
    • Human promoter regulation not directly tested
    • Quantitative contribution of each pathway in physiological contexts unknown
  7. 2010 High

    Identified Src phosphorylation of Y254 as a negative regulatory switch that relocalizes RhoU to endosomes and unloads GTP, providing post-translational control of an otherwise constitutively active enzyme.

    Evidence Y254F/Y254E mutagenesis, Src inhibition, fractionation/imaging, GTP-loading and PAK co-IP, 3D cystogenesis

    PMID:20547754

    Open questions at the time
    • How endosomal relocalization mechanistically unloads GTP not defined
    • Phosphatase reversing Y254 not identified
  8. 2011 High

    Mapped the receptor-coupling mechanism: Grb2/Nck bind RhoU PxxP motifs with high avidity to link activated EGFR on endosomes to RhoU GTP loading, AP-1 activity, and migration, and extended RhoU's role into neural crest and endoderm development.

    Evidence Co-IP, GRB2 RNAi, proline-rich mutagenesis, GTP-loading and AP-1 assays; Xenopus and ES-cell embryo loss/gain of function; ITC binding measurements

    PMID:21156169 PMID:21508312 PMID:21903671 PMID:23183748

    Open questions at the time
    • Whether GTP loading is driven by adaptor-mediated localization or a GEF remains unresolved
    • Selectivity for Grb2/Nck over other SH3 adaptors mechanistically explained only by avidity
  9. 2011 Low

    Identified candidate GAP-family interactors (ARHGAP30, CdGAP) potentially shaping RhoU-driven cytoskeletal output.

    Evidence Binding-partner screen, co-IP/pull-down, overexpression morphology

    PMID:21565175

    Open questions at the time
    • Single co-IP/pulldown screen without reciprocal validation or GAP-activity demonstration on RhoU
    • Functional consequence on RhoU nucleotide state untested
  10. 2012 Medium

    Placed RhoU downstream of NOTCH1 in controlling leukemic cell adhesion and migration, broadening its upstream regulatory inputs.

    Evidence γ-secretase inhibition, Notch1 and RhoU RNAi, active Notch1 expression, adhesion/migration/chemotaxis assays in T-ALL

    PMID:22349824

    Open questions at the time
    • Whether NOTCH1 acts transcriptionally on RhoU not directly shown
    • Effectors mediating the T-ALL phenotype not defined
  11. 2014 Medium

    Demonstrated an in vivo developmental requirement for RhoU acting through Arhgef7b/PAK to control cardiomyocyte junctions and cardiac looping.

    Evidence Zebrafish morpholino, chemical genetic screen, PAK overexpression rescue, epistasis

    PMID:24607366

    Open questions at the time
    • Direct biochemical link between RhoU and Arhgef7b not established
    • Cell-type-specific effectors not resolved
  12. 2015 High

    Revealed proteostatic control of RhoU: PAK4 stabilizes RhoU kinase-independently against Rab40A-Cullin5-mediated ubiquitination, coupling RhoU abundance to adhesion turnover.

    Evidence Ubiquitination assays, Rab40A-Cullin5 and PAK4 co-IPs, PAK4 depletion/kinase-dead, RhoU rescue, adhesion dynamics

    PMID:26598620

    Open questions at the time
    • Structural basis of PAK4 protection vs Rab40A recognition unknown
    • Signals controlling Rab40A-Cullin5 activity toward RhoU undefined
  13. 2019 Medium

    Connected RhoU activity to actomyosin-dependent apoptosis in vivo, showing RhoU loss causes intestinal hyperplasia via elevated RhoA and pMLC-2 and reduced apoptosis.

    Evidence Conditional Rhou knockout mice and DLD-1 RNAi with RhoA activity, pMLC-2, TUNEL, and BrdU readouts

    PMID:30834544

    Open questions at the time
    • Mechanism by which RhoU restrains RhoA not defined
    • Direct apoptotic effector pathway unidentified
  14. 2020 Medium

    Assigned RhoU a role in endosomal fast recycling through PxxP-mediated binding to intersectin-2 on Rab4-positive endosomes.

    Evidence Co-IP, PxxP mutagenesis, transferrin recycling assay, siRNA, Rab4 co-localization

    PMID:32737221

    Open questions at the time
    • Whether GTP state regulates ITSN2 binding not tested
    • Cargo selectivity of RhoU-dependent recycling unknown
  15. 2024 Medium

    Identified C-terminal palmitoylation-dependent homo-oligomerization as a requirement for full RhoU activity, and showed deSUMOylated annexin A6 releases RhoU to enhance AKT signaling and EMT.

    Evidence Co-IP of tagged variants, C-terminal/palmitoylation mutants, PAK activation assay; LC-MS/MS, AnxA6 K579R mutant, p-AKT1 and EMT/migration assays

    PMID:38180080 PMID:38566133

    Open questions at the time
    • Stoichiometry and structural architecture of the oligomer unresolved
    • How AnxA6 sequestration intersects with palmitoylation/oligomerization not addressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how the constitutively GTP-bound RhoU is spatially and temporally switched between its many effectors and locations to produce distinct adhesion, junction, recycling, and apoptotic outputs.
  • No structural model of the autoinhibited vs adaptor-bound state
  • No definitive GAP or GEF demonstrated to set RhoU nucleotide state in cells
  • Integration of palmitoylation, Y254 phosphorylation, oligomerization, and degradation into a single regulatory logic untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 2 GO:0008092 cytoskeletal protein binding 2 GO:0060089 molecular transducer activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005768 endosome 3 GO:0005886 plasma membrane 2 GO:0005856 cytoskeleton 1
Pathway
R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-5357801 Programmed Cell Death 1 R-HSA-5653656 Vesicle-mediated transport 1
Partners
GRB2ITSN2NCK1PAK1PAK4PARD6PYK2RAB40A

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Wrch-1 (RHOU) was identified as a Wnt-1-responsive Cdc42 homolog that activates PAK-1 and JNK-1, induces filopodium formation and stress fiber dissolution, stimulates cell cycle re-entry, and morphologically phenocopies Wnt-1 in transformation of mouse mammary epithelial cells. Functional assays in cell lines: PAK-1/JNK-1 activation assays, morphological analysis, cell cycle analysis, transformation assays Genes & development Medium 11459829
2004 Wrch-1 (RHOU) possesses an extremely rapid intrinsic guanine nucleotide exchange activity (unlike Cdc42) and essentially no GTPase activity, rendering it constitutively GTP-bound. The unique N-terminal extension negatively regulates PAK interaction and transformation, and associates with the Grb2 SH3 domain adaptor protein, which overcomes N-terminal inhibition to promote effector interaction. In vitro biochemical nucleotide exchange and GTPase assays; co-immunoprecipitation with Grb2; N-terminal truncation mutant analysis; transformation assays Current biology : CB High 15556869
2004 Wrch1 (RHOU) has no detectable GTPase activity in vitro and very high intrinsic nucleotide exchange rate. It interacts with PAK1 and NCKβ; the NCKβ interaction is mediated via PxxP motifs in the N-terminal extension binding to the second and third SH3 domains of NCKβ. In vitro GTPase activity assay; pull-down and co-immunoprecipitation identifying PAK1 and NCKβ as binding partners; mapping of interaction to PxxP motifs Experimental cell research High 15350535
2005 Wrch-1 (RHOU) is modified by palmitoylation rather than prenylation, with membrane localization dependent on the second cysteine of the C-terminal CCFV motif. Mutation of this cysteine (C→S) abrogated membrane localization and anchorage-independent transformation. Inhibitors of palmitoylation caused mislocalization, while prenylation inhibitors had no effect. Metabolic labeling with palmitate and isoprenoids; pharmacological inhibition of palmitoylation/prenylation; site-directed mutagenesis of CCFV motif; subcellular fractionation; transformation assays The Journal of biological chemistry High 16046391
2007 RhoU/Wrch-1 localizes to focal adhesions via its C-terminal extension and effector binding loop (N-terminal extension and palmitoylation site dispensable for FA targeting). Activated RhoU reduces focal adhesion number and redistributes them; RhoU silencing increases focal adhesion number. RhoU also localizes to podosomes in osteoclasts and Src-expressing cells. RhoU transiently associated with adhesion structures promotes adhesion turnover and increases cell migration. Fluorescence microscopy; RNAi knockdown; expression of deletion/point mutants; cell migration assays Biology of the cell Medium 17620058
2007 Wrch-1 (RHOU) depletion by siRNA increases focal adhesion formation, inhibits myosin light chain phosphorylation, and inhibits cell migration. Wrch-1 depletion also inhibits Akt and JNK activation. These results place Wrch-1 upstream of myosin light chain phosphorylation and Akt/JNK pathways controlling focal adhesion dynamics and migration. siRNA knockdown; myosin light chain phosphorylation assay; focal adhesion quantification; wound healing migration assay; pharmacological inhibitors of Akt and JNK Journal of cell science Medium 17504809
2007 Wrch1 (RHOU) binds to the nonreceptor tyrosine kinase Pyk2 in a GTP-dependent manner requiring both the N-terminal proline-rich extension and intact effector loop. Pyk2 is required for Wrch1-induced filopodium formation. Src activity is required for formation of the Wrch1-Pyk2 complex and for Wrch1-induced filopodia. Co-immunoprecipitation; GTP-loading experiments with constitutively active/dominant negative mutants; siRNA knockdown of Pyk2; Src inhibitor treatment; morphological analysis Molecular and cellular biology Medium 18086875
2008 Wrch1/RhoU binds integrin β3 cytoplasmic domain and interferes with adhesion-induced Pyk2 and paxillin phosphorylation. Wrch1 expression increases osteoclast precursor aggregation, reduces adhesion onto vitronectin (but not fibronectin), and inhibits M-CSF-induced prefusion osteoclast migration. High Wrch1 activity inhibits podosome belt formation in mature osteoclasts. Co-immunoprecipitation (Wrch1-integrin β3); phosphorylation assays (Pyk2, paxillin); adhesion assays; migration assays; RNAi knockdown; osteoclast differentiation assays The international journal of biochemistry & cell biology Medium 19135548
2008 Activated Wrch-1 (RHOU) binds the cell polarity protein Par6 in a GTP-dependent manner. Activated Wrch-1 negatively regulates tight junction assembly kinetics and disrupts epithelial cystogenesis in 3D culture. A Wrch-1 effector domain mutant that inhibits Par6 binding abrogates tight junction disruption, actin reorganization, and morphogenesis defects, placing Par6 binding as necessary for these effects. Co-immunoprecipitation (GTP-dependent Par6 binding); tight junction assembly assays; 3D cystogenesis assay; effector domain mutant analysis; shRNA knockdown Molecular and cellular biology High 19064640
2009 RhoU transcription is induced by Wnt-1 at the transcriptional level via the non-canonical Wnt/planar cell polarity pathway through JNK activation (independent of β-catenin). RhoU is also transcriptionally induced by gp130 cytokines via STAT3, with two functional STAT3-binding sites identified on the mouse RhoU promoter. Reporter assays; promoter deletion/mutation analysis; ChIP or EMSA for STAT3 binding sites; pathway inhibitor experiments; β-catenin loss-of-function The Biochemical journal Medium 19397496
2010 Wrch-1 (RHOU) is phosphorylated by Src at C-terminal residue Y254. This phosphorylation causes rapid relocalization from plasma membrane to endosomes upon serum stimulation. Y254 phosphorylation decreases active (GTP-bound) Wrch-1, reduces PAK recruitment and activation, and is required for proper cystogenesis in 3D culture. Phospho-deficient Y254F remains plasma membrane-localized and GTP-bound, sustaining PAK activation. Site-directed mutagenesis (Y254F, Y254E); Src genetic/pharmacological inhibition; subcellular fractionation and imaging; GTP-loading assay; PAK co-immunoprecipitation; 3D cystogenesis assay; anchorage-independent growth assay Molecular and cellular biology High 20547754
2010 RhoU activates pathways cooperating with PAK1 and Rac1 in epithelial adhesion, cell spreading, and directional cell migration in cranial neural crest (CNC) cells. Loss or gain of RhoU function in Xenopus impairs CNC cell migration and subsequent craniofacial cartilage differentiation. Gain- and loss-of-function experiments in Xenopus embryos; in vitro cell migration, spreading, and adhesion assays; epistasis with PAK1 and Rac1 Developmental biology Medium 21156169
2011 Rhou (RHOU) maintains the epithelial architecture and F-actin cortical organization of foregut endoderm in vivo. Rhou-deficient embryos show flattened foregut, loss of microvilli, reduced sub-apical F-actin, impaired endoderm differentiation, and reduced c-Jun/AP-1 target gene expression consistent with impaired JNK activity. Rhou knockdown ES cell-derived embryos; embryoid body differentiation; phalloidin staining (F-actin); gene expression analysis Development (Cambridge, England) Medium 21903671
2011 GRB2 couples RhoU to EGFR signaling: after EGF stimulation, RhoU co-localizes with EGFR on endosomes and physically associates with activated EGFR via Grb2 through N-terminal proline-rich motifs. GRB2 knockdown or mutation of proline-rich sequences abolishes the EGFR-RhoU interaction and abrogates EGF-stimulated RhoU GTP loading. RhoU in this complex mediates AP-1 transcriptional activity and cell migration in pancreatic cancer cells. Co-immunoprecipitation; GRB2 RNAi; proline-rich motif mutagenesis; GTP-loading assay; AP-1 reporter assay; cell migration assay Molecular biology of the cell Medium 21508312
2011 ARHGAP30 was identified as a Wrch-1 (RHOU)-interacting protein in a binding-partner screen. CdGAP also binds Wrch-1. Ectopic expression of ARHGAP30 results in membrane blebbing and dissolution of stress fibers and focal adhesions downstream of Wrch-1. Binding-partner screen; co-immunoprecipitation/pull-down; overexpression morphological analysis Biochemical and biophysical research communications Low 21565175
2012 NOTCH1 signaling upregulates RhoU expression in T-ALL cells, and Notch1 or RhoU depletion inhibits T-ALL cell adhesion, migration, and chemotaxis, placing RhoU downstream of NOTCH1 in regulating T-ALL cell migration. γ-secretase inhibitor treatment; Notch1 RNAi; constitutively active Notch1 expression; RhoU RNAi; adhesion, migration, and chemotaxis assays Oncogene Medium 22349824
2013 The N-terminal extension of Wrch1/RhoU contains a central PxxP motif with an essential arginine that mediates high-avidity interactions with full-length Grb2 and Nck1 (but not Crk, c-Src, or p120) in cells, and in vitro. Individual SH3 domains of these adaptors bind with low affinity, but the multivalent full-length proteins achieve tight binding. Sedimentation assays; isothermal titration calorimetry (ITC); co-immunoprecipitation; peptide competition analysis Biological chemistry High 23183748
2014 RhoU regulates cell junctions between cardiomyocytes through the Arhgef7b/PAK kinase pathway to guide atrioventricular canal development and cardiac looping in zebrafish. Loss of RhoU recapitulates cardiac defects seen with ROCK inhibition, and PAK kinase overexpression rescues the RhoU loss-of-function cardiac defect. Zebrafish loss-of-function (morpholino); chemical genetic screen; PAK overexpression rescue; epistasis with Arhgef7b/PAK pathway Developmental biology Medium 24607366
2015 PAK4 protects RhoU from ubiquitination and proteasomal degradation in a kinase-independent manner. RhoU is targeted for ubiquitination by the Rab40A-Cullin 5 E3 ubiquitin ligase complex. PAK4 depletion leads to concomitant loss of RhoU protein; overexpression of RhoU rescues the PAK4 depletion adhesion turnover phenotype. RhoU and PAK4 together drive adhesion turnover and cell migration. Ubiquitination assays; co-immunoprecipitation (Rab40A-Cullin 5 with RhoU; PAK4 with RhoU); PAK4 depletion/kinase-dead mutants; RhoU rescue overexpression; adhesion dynamics assays The Journal of cell biology High 26598620
2019 RhoU loss-of-function in mouse gut epithelium or DLD-1 cells causes hyperplasia through reduced apoptosis and increased proliferation, associated with increased RhoA activity and elevated phosphorylated Myosin Light Chain-2, linking RhoU activity to actomyosin-dependent apoptosis control. Conditional Rhou knockout mice; RNAi in DLD-1 cells; RhoA activity assay; pMLC-2 western blot; TUNEL apoptosis assay; BrdU proliferation assay Biology of the cell Medium 30834544
2020 RhoU interacts with intersectin-1 and intersectin-2 (ITSN1, ITSN2) via the second PxxP motif in its N-terminus binding to ITSN SH3 domains. Silencing of RhoU or ITSN2 (but not ITSN1) increases transferrin accumulation in early endosomes due to a defect in fast vesicle recycling. RhoU and ITSN2 co-localize on Rab4-positive fast recycling endosomes. Co-immunoprecipitation; PxxP motif mutagenesis; fluorescent transferrin uptake/recycling assay; siRNA knockdown; co-localization imaging with Rab4 marker Journal of cell science Medium 32737221
2024 RhoU forms homo-oligomers (homodimers) in cells, mediated by the C-terminal extension; C-terminal palmitoylation is required for self-association. Expression of the isolated C-terminal extension acts as a dominant negative, reducing RhoU-induced PAK activation and causing morphological changes consistent with RhoU inhibition. Self-association is required for full RhoU activity. Co-immunoprecipitation of tagged RhoU variants; C-terminal extension deletion/expression; palmitoylation-deficient mutants; PAK activation assay; cell morphology analysis Journal of cell science Medium 38180080
2024 SUMOylated annexin A6 (AnxA6) binds RhoU; when AnxA6 is deSUMOylated (by SENP1 or K579R mutation), the AnxA6-RhoU interaction is lost, leading to increased RHOU-mediated p-AKT1(Ser473) and facilitation of EMT and cell migration in hepatocellular carcinoma. LC-MS/MS identification of SUMOylation sites; site-directed mutagenesis (K579R); co-immunoprecipitation (AnxA6–RhoU); western blot for p-AKT1; EMT and migration assays Cell communication and signaling : CCS Medium 38566133

Source papers

Stage 0 corpus · 31 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1. Genes & development 182 11459829
2005 Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif. The Journal of biological chemistry 69 16046391
2004 Atypical mechanism of regulation of the Wrch-1 Rho family small GTPase. Current biology : CB 67 15556869
2015 PAK4 promotes kinase-independent stabilization of RhoU to modulate cell adhesion. The Journal of cell biology 63 26598620
2004 Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects. Experimental cell research 59 15350535
2007 Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration. Biology of the cell 52 17620058
2008 The Rho GTPase Wrch1 regulates osteoclast precursor adhesion and migration. The international journal of biochemistry & cell biology 51 19135548
2009 The RhoU/Wrch1 Rho GTPase gene is a common transcriptional target of both the gp130/STAT3 and Wnt-1 pathways. The Biochemical journal 47 19397496
2002 Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta-estradiol in MCF-7 cells. International journal of oncology 44 11894124
2017 Regulation and functions of RhoU and RhoV. Small GTPases 43 29189096
2008 The transforming Rho family GTPase Wrch-1 disrupts epithelial cell tight junctions and epithelial morphogenesis. Molecular and cellular biology 43 19064640
2007 The atypical Rho family GTPase Wrch-1 regulates focal adhesion formation and cell migration. Journal of cell science 43 17504809
2011 Rhou maintains the epithelial architecture and facilitates differentiation of the foregut endoderm. Development (Cambridge, England) 42 21903671
2012 Analysis of Rho GTPase expression in T-ALL identifies RhoU as a target for Notch involved in T-ALL cell migration. Oncogene 36 22349824
2022 LncRNA SNHG16 promotes development of oesophageal squamous cell carcinoma by interacting with EIF4A3 and modulating RhoU mRNA stability. Cellular & molecular biology letters 34 36221055
2011 GRB2 couples RhoU to epidermal growth factor receptor signaling and cell migration. Molecular biology of the cell 32 21508312
2010 Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src. Molecular and cellular biology 31 20547754
2010 Activity of the RhoU/Wrch1 GTPase is critical for cranial neural crest cell migration. Developmental biology 30 21156169
2007 The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics. Molecular and cellular biology 27 18086875
2011 ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion. Biochemical and biophysical research communications 23 21565175
2014 The atypical Rho GTPase, RhoU, regulates cell-adhesion molecules during cardiac morphogenesis. Developmental biology 21 24607366
2018 The small GTPase RhoU lays downstream of JAK/STAT signaling and mediates cell migration in multiple myeloma. Blood cancer journal 20 29440639
2019 Identification of CDK6 and RHOU in Serum Exosome as Biomarkers for the Invasiveness of Non-functioning Pituitary Adenoma. Chinese medical sciences journal = Chung-kuo i hsueh k'o hsueh tsa chih 19 31601299
2015 Atypical RhoV and RhoU GTPases control development of the neural crest. Small GTPases 13 26555387
2013 SH3-mediated targeting of Wrch1/RhoU by multiple adaptor proteins. Biological chemistry 13 23183748
2008 Dynamic expression patterns of RhoV/Chp and RhoU/Wrch during chicken embryonic development. Developmental dynamics : an official publication of the American Association of Anatomists 13 18351666
2024 SUMOylation of annexin A6 retards cell migration and tumor growth by suppressing RHOU/AKT1-involved EMT in hepatocellular carcinoma. Cell communication and signaling : CCS 12 38566133
2019 The atypical RhoU/Wrch1 Rho GTPase controls cell proliferation and apoptosis in the gut epithelium. Biology of the cell 12 30834544
2011 Atypical RhoV and RhoU GTPases control development of the neural crest. Small GTPases 11 22545228
2020 The atypical Rho GTPase RhoU interacts with intersectin-2 to regulate endosomal recycling pathways. Journal of cell science 6 32737221
2024 RhoU forms homo-oligomers to regulate cellular responses. Journal of cell science 4 38180080

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