Ask about this productRelated genes to: Twist1 antibody
- Gene:
- TWIST1 NIH gene
- Name:
- twist family bHLH transcription factor 1
- Previous symbol:
- ACS3, BPES3, TWIST, CRS
- Synonyms:
- SCS, H-twist, BPES2, bHLHa38, CRS1
- Chromosome:
- 7p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-01
- Date modifiied:
- 2016-10-05
Related products to: Twist1 antibody
Related articles to: Twist1 antibody
- Post-burn hypertrophic scar (HTS) formation is influenced by the dynamic balance between keratinocyte proliferation and differentiation, a process critical for maintaining skin homeostasis. Serine/threonine kinase 33 (STK33) has emerged as a potential therapeutic target in oncology. However, its role in HTS formation remains unclear, and its effects on keratinocytes are poorly understood. We isolated human HTS-derived keratinocytes (HTSKs) from post-burn HTS tissues and treated them with ML281, originally developed as an STK33 inhibitor. We examined markers associated with keratinocyte phenotypes and functions, including proliferation (proliferating cell nuclear antigen, c-Myc, keratins 5, 14, 6, 16, and 17), epithelial-mesenchymal transition (EMT; snail1, slug, twist1, e-cadherin, n-cadherin, and vimentin), differentiation (keratins 1 and 10, involucrin, loricrin, Notch1, p21, and p27), and apoptosis (cytochrome c, cleaved caspase3, Bid, Bad, Bax, and Bcl-2). mRNA and protein expression levels were assessed using reverse transcription-quantitative PCR, Western blotting, and immunocytochemistry. In HTSKs, ML281 increased STK33 enzymatic activity and STK33 mRNA and protein expression, rather than inhibiting STK33 activity. ML281 treatment reduced the expression of proliferation-associated markers, promoted an EMT-associated phenotype, modulated the expression of differentiation-associated markers, and induced apoptosis-associated changes. Collectively, these findings suggest that ML281 alters post-burn HTSK phenotypes associated with proliferation, EMT, differentiation, and apoptosis. - Source: PubMed
Publication date: 2026/09/17
Zheng Ya XinCui Hui SongLee You RaJoo So YoungCho Yoon SooKwak In SukSeo Cheong Hoon - TWIST1 is a deeply conserved basic helix-loop-helix (bHLH) transcription factor that has emerged as a central transcriptional regulator bridging developmental biology and cancer pathogenesis. This key regulator orchestrates mesoderm formation, neural crest migration, and craniofacial morphogenesis through precise dimerization-dependent mechanisms. The TWIST1 bHLH domain mediates DNA binding at E-box motifs (CANNTG), with its regulatory role determined by homodimer versus E-protein heterodimer formation. Recent reports demonstrate that post-translational modifications (PTMs) are critical for TWIST1 activity: diacetylation at K73/K76 by TIP60 recruits BRD8 to activate mesenchymal and MYC targets, whereas non-acetylated TWIST1 recruits the NuRD repressor complex to silence epithelial genes. Aurora kinase A (AURKA) phosphorylation at three sites stabilizes TWIST1, promotes homodimerization, and drives chemoresistance, while SETD6-mediated K33 methylation enhances EZH2 occupancy and H3K27me3 deposition at the LINC-PINT locus. Germline loss-of-function mutations clustered in the bHLH domain cause Saethre-Chotzen syndrome (SCS), an autosomal dominant craniosynostosis disorder characterized by protein degradation or impaired nuclear localization. Therapeutic targeting TWIST1 remains challenging due to the absence of deep binding pockets, but emerging strategies include harmine (a β-carboline alkaloid)-mediated proteasomal degradation, BRD4/TIP60/BRD8 axis inhibition, and transcription factor-targeted proteolysis-targeting chimeras (TF-PROTACs) employing DNA oligonucleotide warheads linked to E3 ligase ligands. This review summarizes classic and recent findings on structural biology, PTM networks, mutation landscapes, oncogenic mechanisms, and therapeutic frontiers, highlighting TWIST1 as a target for precision oncology and therapy. - Source: PubMed
Publication date: 2026/09/24
Pires Bruno Ricardo BarretoFerreira Gerson MouraAbdelhay Eliana - Craniosynostosis, resulting from the premature fusion of one or more cranial sutures, often requires invasive surgery for treatment. Currently, the spatiotemporal regulation of calvarial ossification during suture development is largely focused on cellular and molecular patterns. Using physicochemical imaging and nanomechanical mapping, we identified a unidirectional osteo-periosteal interface characterized by calcium phosphate deposition gradient during early postnatal calvarial development. Lineage tracing and dynamic bone formation assays revealed that Mmp13-positive osteoprogenitors, derived from Erg-expressing suture mesenchyme, establish this osteo-periosteal interface and drive asymmetric calvarial osteogenesis in mice. In the Twist1 craniosynostosis model, mineralization patterns initially resembled those of wild-type mice; however, misregulation of the PAK1/MMP13/BMP7 signaling cascade at the dura side triggered bilateral mineralization within the coronal suture, ultimately leading to bone fusion. Importantly, early localized inhibition of MMP13 overactivation, achieved by applying CL-82198 (a small-molecule MMP13 inhibitor) in a thin 20% gelatin methacryloyl (GelMA) hydrogel-based 'Suture Patch', preserved coronal suture patency in Twist1 mutants via a minimally invasive surgical procedure. Our work identifies a unilateral osteo-periosteal interface that is critical for coronal suture patency, reveals the regulatory role of non-cellular components in calvaria development, and proposes a minimally invasive strategy to preserve asymmetric osteogenesis in cranial sutures for the treatment of craniosynostosis. STATEMENT OF SIGNIFICANCE: Craniosynostosis is a premature skull suture fusion that currently requires invasive surgery. We discover a unidirectional mineralization gradient driven by Mmp13 osteoprogenitors. In a craniosynostosis model, this asymmetric process becomes bilateral and pathological. Leveraging this insight, we engineer a 200-μm hydrogel "Suture Patch" that delivers a small-molecule Mmp13 inhibitor locally. A single application in newborn mice preserves suture patency in 80% of treated animals, corrects skull deformity, and restores progenitor pools-without surgery. Our work integrates advanced materials characterization, single-cell biology, and translational bioengineering to provide both a fundamental revision of suture development and a practical, minimally invasive biomaterial therapy for the debilitating pediatric disorder. - Source: PubMed
Publication date: 2026/09/24
Meng HongxuWang XinyiWu BoxuanJiang YingqiDong YuningZhang TianyiChen BingqianLi HanzhangChen TaozehanLi WenyueWang XiaozhaoLan XinZhao TianruiHu HuanHuang WenwenGavara NúriaOuyang HongweiYuan Yuan - Precise and rapid control over cellular protein levels is essential to dissect complex biological systems. Chemical genetic approaches such as dTAG, in which a target is fused to a degron tag (FKBP12F36V) and degraded upon small molecule-mediated recruitment of E3 ligases, have enabled rapid and tunable control over protein abundance. However, no analogous tool exists to precisely increase protein levels and actively reverse dTAG-mediated degradation. Here, we developed heterobifunctional small molecules (dubTAGs) that stabilize FKBP12F36V-tagged proteins by recruiting endogenous deubiquitinases. Utilizing stem cell-derived cranial neural crest cells (CNCCs) in which the transcription factors SOX9 or TWIST1 are endogenously tagged with FKBP12F36V, we identified OTUB1- or USP7-recruiting heterobifunctional molecules that demonstrated effective target stabilization and ternary complex formation. We demonstrate that dubTAG-mediated protein stabilization is dependent on deubiquitinase recruitment, target-specific, and can tunably and rapidly reverse dTAG-mediated degradation. We applied dubTAGs to assess how stabilizing endogenous SOX9 impacts chromatin accessibility in CNCCs, finding both monotonic and non-monotonic regulatory element responses that are driven by distinct sequence features. dubTAGs are readily applicable tools for investigating the effects of elevated protein levels and tunably reversing targeted degradation, enabling new approaches to study protein dosage effects in development, disease, and therapeutic discovery. - Source: PubMed
Publication date: 2026/09/18
Guharajan SunilSong XiangyangWu QiongSengupta SachiWei WenyiXiong YanJin JianNaqvi Sahin - Benzo[a]pyrene (BaP) is a polycyclic fragrant hydrocarbon contaminant commonly establish throughout the surroundings. The International Agency for Research on Cancer has classified it as a Group 1 carcinogen; however, its exact contribution to the onset of prostate cancer (PCa) is still not well defined. This study systematically explores the mechanism underlying the association between BaP exposure and prostate cancer using approaches including network toxicology, machine learning, transcriptomic validation, immune infiltration assessment, single-cell analysis, molecular docking and external validation. The results showed that BaP and prostate cancer shared 975 overlapping targets, which were predominantly enriched in signaling pathways such as PI3K-Akt. Four core genes were screened out through differential analysis and machine learning, namely CAV1, TWIST1, PRKCA, and GDF15. Transcriptome verification showed that TWIST1 and GDF15 were up-regulated, CAV1 and PRKCA were down-regulated, and the AUC of the four-gene combined diagnosis reached 0.990. Core genes are associated with cellular growth and immune cell recruitment, and single-cell sequencing verified their specific cellular distribution and immunological shifts. Molecular docking showed that BaP binds well to the core target. External validation confirmed that BaP may promotes the progression of PCa, with upregulated expression of GDF15 and downregulated expression of PRKCA in PCa. In conclusion, BaP may promote the development of PCa by regulating pathways such as CAV1, TWIST1, GDF15 and PRKCA. - Source: PubMed
Publication date: 2026/09/23
Zhu SiqiLi ZhuangJiang KehuaSun FaZhu Jianguo