| 2010 |
WTIP (along with LIMD1 and Ajuba) localizes to processing bodies (P-bodies) and binds Ago1/2, RCK, Dcp2, and eIF4E in vivo, acting as a molecular link between the translationally inhibited eIF4E-m7GTP-5' cap and Ago1/2 within the miRISC complex to facilitate miRNA-mediated (but not siRNA-mediated) gene silencing via an inhibitory closed-loop complex. |
Co-immunoprecipitation, m7GTP cap-binding assay, P-body localization imaging, knockdown functional assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20616046
|
| 2010 |
Upon LPS-induced podocyte injury, WTIP translocates from cell contacts to the nucleus via a mechanism requiring JNK activity, assembly of a JNK-interacting protein 3/dynein scaffolding complex, intact microtubule networks, and dynein motor activity. Loss of WTIP from cell contacts alters podocyte morphology and actin assembly. |
Live imaging, cellular fractionation, pharmacological inhibition of JNK/dynein/microtubules, shRNA knockdown, co-immunoprecipitation of JIP3-dynein complex |
The Journal of biological chemistry |
High |
20086015
|
| 2011 |
WTIP regulates podocyte actin dynamics and adherens junction assembly: it targets focal adhesions in isolated cells and shifts to adherens junctions upon cell-cell contact; knockdown disrupts actin stress fiber formation, focal adhesion maturation, and stable adherens junction assembly. WTIP overexpression induces RhoA-dependent stress fibers and directly interacts with the RhoA-specific GEF ARHGEF12. |
shRNA knockdown, overexpression, RhoA inhibition (C3 toxin, ROCK inhibitor), co-immunoprecipitation, cell surface biotinylation |
American journal of physiology. Renal physiology |
High |
21900451
|
| 2009 |
WTIP physically interacts with the intracellular domain of the receptor tyrosine kinase Ror2; full-length Ror2 recruits WTIP to the cell membrane, while a disease-causing Ror2 mutant fails to do so. WTIP inhibits canonical Wnt signaling in mammalian cells and in Xenopus embryos. |
Co-immunoprecipitation, cell membrane localization assay, Wnt/β-catenin luciferase reporter assay, Xenopus overexpression |
Biochemical and biophysical research communications |
Medium |
19785987
|
| 2012 |
In zebrafish, Wtip is enriched at the basal body; wtip knockdown causes pronephric cyst formation, mitotic spindle orientation defects (in anterior/middle pronephros), cloaca malformation with reduced ciliated cells, loss of striated rootlet from basal bodies, and impaired cilia motility. Genetic interaction with vangl2 (a core PCP protein) was demonstrated. |
Morpholino knockdown, immunolocalization, spindle orientation assay, cilia motility analysis, genetic epistasis (double knockdown) |
Biology open |
High |
23213452
|
| 2016 |
Nephrin signaling suppresses Hippo pathway activity through WTIP: phosphorylated nephrin recruits Nck, which sequesters WTIP and its binding partner Lats1, resulting in decreased phospho-activation of Lats1. Upon nephrin dephosphorylation during podocyte injury, Lats1 is rapidly activated, preceding YAP downregulation. |
Mutational analysis of Nck/nephrin interaction, co-immunoprecipitation, mouse podocyte injury model with phospho-Lats1 and YAP quantification |
The Journal of biological chemistry |
High |
27033705
|
| 2016 |
Wtip physically associates with Prickle3 and cooperates with it to regulate ciliogenesis; Wtip is required for basal body organization in Xenopus GRP cells, and co-depletion or interference phenotypes link Wtip to Prickle3-mediated cilia growth. |
Co-immunoprecipitation, morpholino knockdown in Xenopus, immunolocalization of basal body markers (γ-tubulin, Nedd1) |
Scientific reports |
Medium |
27062996
|
| 2018 |
Wtip regulates actomyosin contractility and apical constriction during neural tube closure in Xenopus: depletion inhibits apical constriction in neuroepithelial cells and causes neural tube defects. The C-terminal LIM domain fragment of Wtip physically associates with Shroom3 and interferes with Shroom3-induced apical constriction. Wtip junctional distribution is reorganized by myosin II activity, indicating tension-sensitive localization. |
Morpholino depletion, fluorescent protein tagging/live imaging, co-immunoprecipitation, myosin II inhibition (blebbistatin) |
Journal of cell science |
High |
29661847
|
| 2014 |
WTIP directly interacts with ASXL2 and represses ASXL2-mediated activation of retinoic acid-dependent transcription in HeLa cells, blocking ASXL2's stimulatory effect on retinoic acid signaling. |
Yeast two-hybrid, co-immunoprecipitation, luciferase reporter assay |
Biochemical and biophysical research communications |
Medium |
25065743
|
| 2015 |
WTIP physically interacts with ASXL1; in Asxl1-null mouse kidneys, defects in podocyte morphology and upregulation of Wt1/Wtip target genes are observed, implicating Asxl1 in maintaining podocyte structure via its association with Wtip. |
Co-immunoprecipitation, Asxl1 knockout mouse analysis, target gene expression |
Biochemical and biophysical research communications |
Medium |
26385183
|
| 2013 |
Dendrin physically interacts with WTIP (and Gadd45a) at the podocyte slit diaphragm, as demonstrated by yeast two-hybrid and co-immunoprecipitation. Dendrin relocalizes to the nucleus in adriamycin nephropathy, paralleling WTIP nuclear translocation behavior. |
Yeast two-hybrid, co-immunoprecipitation, dendrin knockout mouse, immunolocalization |
PloS one |
Medium |
24376653
|
| 2016 |
WTIP interacts with BRCA2 (amino acids 2750–2864) and is required for BRCA2 centrosome localization; knockdown of WTIP abolishes BRCA2 centrosomal localization and causes abnormal cell division in HeLa S3 cells. |
Yeast two-hybrid, co-immunoprecipitation, GST pull-down, shRNA knockdown, immunofluorescence |
Archives of gynecology and obstetrics |
Medium |
27535760
|
| 2018 |
A UBA2-WTIP fusion gene (containing UBA2 N-terminal domains fused to WTIP C-terminal LIM domains) was identified in AML; ectopic expression enhances cell proliferation, induces phosphorylation of STAT3, STAT5, and ERK1/2, and abrogates WTIP-mediated P-body formation. |
RT-PCR, Sanger sequencing, ectopic expression in KG-1a cells, proliferation assay, Western blot for phospho-signaling, P-body formation assay |
Experimental cell research |
Medium |
30179602
|
| 2021 |
WTIP induces apoptosis in AML cells through transcriptional upregulation and nuclear translocation of FOXO3a; WTIP directly interacts with FOXO3a, activates FOXO3a transcriptionally, which increases PUMA expression and activates the intrinsic apoptotic pathway. |
Overexpression/knockdown, co-immunoprecipitation (WTIP-FOXO3a), luciferase reporter, in vitro and in vivo proliferation/apoptosis assays |
Cell death & disease |
Medium |
34930905
|
| 2021 |
WTIP N-terminal domain physically associates with SSX2IP (a centriolar satellite protein/cell junction component); the two proteins form mixed aggregates when overexpressed, and double depletion of Wtip and SSX2IP in Xenopus embryos shows functional interaction during neural tube closure. |
Targeted proximity biotinylation (TPB), co-immunoprecipitation, colocalization imaging, double morpholino depletion |
PloS one |
Medium |
34710136
|
| 2022 |
WTIP interacts with ARHGEF12 (a RhoA-specific GEF) through LIM and PDZ-binding domains with high affinity; this interaction is proposed to regulate slit diaphragm and foot process function through Rho effector proteins. Wtip gene trap homozygotes are embryonic lethal. |
Co-immunoprecipitation, domain mapping, Wtip gene trap mouse model |
American journal of physiology. Renal physiology |
Medium |
35862649
|
| 2022 |
Overexpression of WTIP in MCF10A cells competes with LIMD1 for junctional localization, reduces junctional localization of LATS1, and is associated with increased YAP1 phosphorylation and decreased YAP1 nuclear localization, suggesting WTIP cannot efficiently recruit Lats kinases to junctions (unlike LIMD1) and may act as a tumor suppressor partly by competing with LIMD1. |
Overexpression in MCF10A cells, immunofluorescence quantification of junctional localization, YAP1 phosphorylation and nuclear localization assay |
microPublication biology |
Medium |
36439396
|
| 2022 |
WTIP knockdown in neonatal rat ventricular myocytes causes cardiomyocyte hypertrophy; a disease-causing variant WTIP p.Y233F disrupts binding to a Wnt signaling protein, causes increased resting calcium and cellular hypertrophy in iPSC-derived cardiomyocytes (ameliorated by verapamil), linking WTIP to calcium dysregulation and cardiac hypertrophy. |
lentiviral shRNA knockdown in neonatal rat cardiomyocytes, morpholino knockdown in zebrafish, iPSC-derived cardiomyocyte characterization, calcium imaging, verapamil rescue |
Circulation. Genomic and precision medicine |
Medium |
35671065
|
| 2025 |
WTIP interacts with PP2A to inhibit T308 phosphorylation and kinase activity of AKT, thereby suppressing stemness and chemoresistance in gastric cancer. TET2 and PATZ1 cooperate to transcriptionally activate WTIP expression, and this TET2-WTIP axis is frequently silenced in gastric cancer. |
Co-immunoprecipitation (WTIP-PP2A), AKT kinase activity assay, TET2/PATZ1 transcriptional activation assays, shRNA knockdown functional assays |
Neoplasia (New York, N.Y.) |
Medium |
40279682
|
| 2016 |
In zebrafish, Wtip protein localizes to the basal body of proepicardial organ (PE) cells; Wtip signaling in conjunction with WT1 is essential for PE specification. Wtip knockdown disrupts cardiac looping, left-right asymmetry, and atrioventricular boundary formation. |
Morpholino knockdown in zebrafish, mRNA overexpression, immunolocalization, PE marker expression analysis |
Molecular medicine reports |
Medium |
27484451
|