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Disruption of Snail expression in follicle stem cells compromises proliferation, but not maintenance. FSCs with excessive Snail expression had increased proliferation and lifespan, accompanied by a moderate decrease inE-cadherin expression (required for adhesion of FSCs to their niche) at the junction between their adjacent cells, indicating a conserved role of Snail in E-cadherin (show CDH1 Proteins) inhibition.
during gastrulation of Drosophila embryos, Sna expression downregulates polarity protein Baz which in turn results in junction disassembly at protein levels.
evidence for mechanosensitivity of cell-cell junctions and implications that myosin-mediated tension can prevent Snail-driven Eepithelial-mesenchymal transitions
Snail can potentiate enhancer activation by collaborating with different activators, providing a new mechanism by which Snail regulates development.
Rapid transcription kinetics and negative autoregulation are responsible for the remarkable homogeneity of snail expression and the coordination of mesoderm invagination.
Study shows that Sna represses transcription of pbl in the mesoderm primordium of D. melanogaster via one or more Sna-binding sites, which are conserved among species of the Drosophila genus, but not in the mosquito, correlating with the different modes of gastrulation in the different genuses.
Complex interactions between cis (show CISH Proteins)-regulatory modules in native conformation are critical for Drosophila snail expression.
The Snail repressor positions Notch (show NOTCH1 Proteins) signaling in the Drosophila embryo.
results show that Sna has a positive regulatory function on sim (show SIM2 Proteins) expression in the presumptive mesectoderm; this positive effect of Sna depends on the Su(H (show RBPJ Proteins))-binding sites within the sim (show SIM2 Proteins) promoter, suggesting that Sna regulates Notch (show NOTCH1 Proteins) signaling
snail is required for Drosophila gastrulation and is not replaceable by Escargot or Worniu.
The transcription factor Snail1 is essential for tissue separation, enabling paraxial protocadherin (PAPC (show PCDH8 Proteins)) to promote tissue separation through novel functions.
Interaction with Snail1/2, and Twist function more generally, is regulated by GSK-3-beta-mediated phosphorylation of conserved sites in the WR domain.
the same E3 ubiquitin ligase (show MUL1 Proteins) known to regulate Snail family proteins, Partner of paired (Ppa (show FBXL14 Proteins)), also controlled Twist stability and did so in a manner dependent on the Twist WR-rich domain
Snail-1 might play an important role in the progression of bladder cancer
Study demonstrated in human breast cancer samples that MDM2 (show MDM2 Proteins) induces epithelial-to-mesenchymal transition by enhancing Snail expression in vitro and in vivo.
Amla extract (Emblica officinalis, AE) decreases the gene and protein expression of IGF1R (show IGF1R Proteins), a target of miR (show MLXIP Proteins)-375, and SNAIL1, a transcription factor that represses E-cadherin (show CDH1 Proteins) expression.
The results demonstrate that knockdown of Snail can inhibit the inhibits epithelial-mesenchymal transition process of laryngeal squamous cell carcinoma cells through the vitamin D receptor (show VDR Proteins) signaling pathway in vitro.
By repressing FOXA family members, SNAIL1 targets transcription factors at strategically important positions in gene-regulatory hierarchies, which may facilitate transcriptional reprogramming during EMT (show ITK Proteins).
Results show that Snail is a direct target of miR (show MLXIP Proteins)-137 and miR (show MLXIP Proteins)-34a in ovarian cancer cells.
Results show that Snail1 transcriptional activation is regulated by SOX3 (show SOX3 Proteins) via binding to its promoter region in osteosarcoma cells promoting migration, invasiveness, and EMT (show ITK Proteins).
Cten (show TNS4 Proteins)-Snail signaling pathway contributes to cell motility in colorectal cancer (CRC (show CALR Proteins)), mediated by the stabilization of Snail protein.
Mechanistic investigations found that quercetin suppressed Snail-dependent Akt (show AKT1 Proteins) activation by upregulating maspin (show SERPINB5 Proteins) and Snail-independent a disintegrin and metalloproteinase (ADAM) 9 (show ADAM9 Proteins) expression pathways to modulate the invasive ability of NSCLC cells
There was a significant stepwise increase of upgrading rate according to Snail1 expression in DCIS cells: weak 9%, intermediate 26%, and strong 55%, respectively.
a Snail1-ATGL (show PNPLA2 Proteins) axis that regulates adipose lipolysis and fatty acid release, is reported.
A20 (show TNFAIP3 Proteins) promotes metastasis of aggressive basal-like breast cancers through multi-monoubiquitylation of Snail1.
Metagenomic analysis revealed direct correlation between PPARGC1A, SNAI1, and metastatic lung disease.
both Snail and Slug are able to form binary complexes with either YAP (show YAP1 Proteins) or TAZ (show TAZ Proteins) that, together, control YAP (show YAP1 Proteins)/TAZ (show TAZ Proteins) transcriptional activity and function throughout mouse development.
results demonstrate that skeletal stem/stromal cell mobilize Snail/Slug-YAP (show YAP1 Proteins)/TAZ (show TAZ Proteins) complexes to control stem cell function
these results might suggest that calcineurin inhibitor (show RCAN1 Proteins)-induced tubular SNAI1 protein cytoplasmic accumulation, possibly because of impaired SNAI1 proteasomal degradation and nuclear translocation, might be a sign of a diseased profibrotic epithelial phenotype.
Snail1 as a molecular bypass that suppresses the anti-proliferative and pro-apoptotic effects exerted by wild-type p53 (show TP53 Proteins) in breast cancer
Snail1 deficiency modified the phenotype of pancreatic tumors .
miR (show MLXIP Proteins)-200 promotes the mesenchymal to epithelial transition by suppressing multiple members of the Zeb2 and Snail1 transcriptional repressor complexes, such as Smad2 (show SMAD2 Proteins) and Smad5 (show SMAD5 Proteins).
show that Snail1-induced fibrosis can be reversed in vivo and that obstructive nephropathy can be therapeutically ameliorated in mice by targeting Snail1 expression
The Drosophila embryonic protein snail is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The nuclear protein encoded by this gene is structurally similar to the Drosophila snail protein, and is also thought to be critical for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2.
snail homolog 1
, snail like protein
, Protein snail-like protein 1
, snail homolog 1 (Drosophila)
, snail 1 homolog
, zinc-finger transcription factor Snail
, protein Xsnail
, protein snail homolog Sna
, protein xSna
, snail protein
, zinc finger protein with snail domain similar to escargot
, transcription factor protein
, snail zinc finger protein
, snail-like protein 1
, protein sna
, protein snail homolog 1
, snail 1 zinc finger protein
, snail 1, zinc finger protein
, zinc finger protein SNAI1