Ask about this productRelated genes to: Twf1 Blocking Peptide
- Gene:
- TWF1 NIH gene
- Name:
- twinfilin actin binding protein 1
- Previous symbol:
- PTK9
- Synonyms:
- A6
- Chromosome:
- 12q12
- Locus Type:
- gene with protein product
- Date approved:
- 1997-12-17
- Date modifiied:
- 2016-04-25
Related products to: Twf1 Blocking Peptide
Related articles to: Twf1 Blocking Peptide
- Twinfilin-1 (TWF1) is a cellular protein that binds actin, phosphoinositides, and capping protein. Although multiple studies have reported the tumor-regulatory role of TWF1, a comprehensive and critical review of these findings remains unavailable. This review addresses this gap by consolidating current evidence on the tumor-modulatory functions of TWF1. The literature indicates that dysregulation of TWF1 or its actin-binding activity can promote carcinogenesis by influencing interleukin-11/signal transducer and activator of transcription 3, protein kinase B, epithelial-to-mesenchymal transition, or autophagy. The mechanisms by which TWF1 regulates tumorigenesis are tissue-dependent and vary across different tissues. At least 10 microRNAs, 2 long noncoding RNAs, and 1 circular RNA have been identified as interacting with TWF1, either directly or indirectly, to regulate its expression and tumor-controlling function. High TWF1 expression has been observed in at least 8 types of solid tumors, but not in liquid cancers, highlighting its potential as a diagnostic biomarker for solid tumors. Furthermore, its increased expression in solid tumors can help predict cancer patient prognosis. However, despite these findings, the translational potential of TWF1 requires further validation through in-depth mechanistic studies and large-scale clinical trials, as current evidence is primarily derived from bioinformatics analyses, preclinical studies, or small prospective cohorts. Once the tumor-promoting role of TWF1 is confirmed, future research should then evaluate its sensitivity and suitability as a biomarker or therapeutic target. SIGNIFICANCE STATEMENTS: Twinfilin-1 (TWF1) regulates various cellular processes that contribute to solid cancer cell proliferation, metastasis, and resistance to treatment. These functions suggest that TWF1 has translational potential as both a biomarker and a therapeutic target in cancer management. - Source: PubMed
Publication date: 2026/06/04
Chong Zhi-Xiong - Obesity involves white adipose tissue (WAT) expansion via hyperplasia and hypertrophy. Impaired adipocyte proliferation leads to pathological hypertrophy, inflammation and metabolic dysfunction. Aberrant F‑actin turnover disrupts proliferation/differentiation. Twinfilin‑1 (Twf1) regulates actin dynamics and cell proliferation/differentiation, but its role in adipocytes is unknown. Obese mice were induced by high‑fat diet (HFD) and weight loss by calorie restriction. Inguinal, epididymal and scapular adipose tissues were collected. Proteomics used pressure cycling, DDA library building and DIA quantification. Twf1 expression was validated by RT‑qPCR and Western blot. In C3H10T1/2 preadipocytes, Twf1 knockdown and overexpression were established. Differentiation was induced with dexamethasone, rosiglitazone, insulin and IBMX. Adipogenesis and proliferation were assessed by RT‑qPCR, Western blot, Oil Red O and CCK8. Nuclear‑cytoplasmic fractionation evaluated Yap localization and HIPPO activity. HFD mice showed weight gain, dyslipidemia and adipocyte hypertrophy, reversed by weight loss. Proteomics identified 43 proteins intersecting obesity, weight loss, and actin‑related datasets; Twf1 was upregulated in obese epididymal/inguinal fat and downregulated after weight loss. In C3H10T1/2 cells, Twf1 knockdown enhanced white adipocyte differentiation (upregulated Pparg2, Fsp27, Fabp4) and proliferation (2.28‑fold vs. control), promoted Yap nuclear accumulation, and inhibited HIPPO signalling. Twf1 overexpression reduced differentiation, lipid droplets, and proliferation (to 44.7% of control). Twf1 is upregulated in white/beige adipose tissue of obese mice and downregulated after weight loss. Twf1 knockdown promotes Yap nuclear accumulation, inhibits HIPPO and enhances adipocyte proliferation and white adipocyte maturation, indicating a key role in obesity development. - Source: PubMed
Publication date: 2026/06/24
Kai ChenXu HaiyanLv SuzhenHuang Xin - Forty-five fungal strains from decomposing wood, representing eight genera, were isolated. Among them, 27 cellulolytic strains were identified. The genera Trichoderma, Penicillium, and Phanerochaete (6, 2, and 4 isolates, respectively) demonstrated the highest cellulase production. The isolates TW-25, TW-28, and TW-33 exhibited superior enzyme activities, CMCase (5.4-6.5 U/mL), FPase (3.2-3.8 U/mL), pNPCase (2.6-3.0 U/mL), and pNPGase (3.5-4.0 U/mL) and were selected for further study. Internal transcribed spacer (ITS) region sequencing, combined with phenotypic characteristics, identified these strains as Trichoderma sp. TW-25, Trichoderma sp. TW-28, and Penicillium sp. TW-33. Maximum protoplast release was observed in Trichoderma sp. TW-25 (3.6 × 10⁶ protoplasts/mL), followed by Trichoderma sp. TW-28 (3.0 × 10⁶ protoplasts/mL) and Penicillium sp. TW-33 (2.8 × 10⁶ protoplasts/mL). Fusion frequencies were 2.8 × 10⁻³ for TW-25 × TW-28, 2.0 × 10⁻³ for TW-25 × TW-33, and 1.8 × 10⁻³ for TW-28 × TW-33. A total of 13 colonies obtained from TW-25 × TW-28, and 18 from intergeneric fusions (10 from TW-25 × TW-33 and 8 from TW-28 × TW-33). The cellulase activity of the fusants TWF1/1, TWF1/6, and TWF2/5 was the same as TW-25 and the fusants TWF1/3 and TWF3/2 the same as TW-28 while none of the fusants had the cellulase activity of TW-33. Fusants differed from their parental strains in their DNA content (3.25-3.65 µg/mg dry weight) and showed high cellulase activities in general. Among them, TWF1/10 demonstrated the highest enzymatic activity, producing CMCase, FPase, pNPCase, and pNPGase (10.5, 6.5, 5.8, and 7.5 U/mL), respectively, followed by TWF1/13, TWF2/8, TWF2/10, and TWF3/8. DNA banding patterns of TWF1/10, TWF1/13, TWF2/8, TWF2/10, and TWF3/8, analyzed using four RAPD and three ISSR primers, differed from their parental strains, except for ISSR-3 with fusants TWF1/10 and TWF1/13. These variations underscore the effectiveness of interspecific and intergeneric protoplast fusion. The supernatant of the hybrid strain TWF1/10 was concentrated and purified via ultrafiltration, and SDS-PAGE and zymogram assays confirmed its cellulase activity using CMC as the substrate. - Source: PubMed
Publication date: 2025/10/24
Alsarraf Mohammad JAl-Wahaibi Aisha S MStephenson Steven LAlshaikh Najla AAmeen Fuad - To investigate the molecular mechanisms underlying how Twinfilin actin-binding protein 1 (TWF1) drives the malignant progression of head and neck squamous cell carcinoma (HNSCC). - Source: PubMed
Publication date: 2025/10/14
Yang YingshunYang KaichengPeng ShixiongMan ShashaChen He - Reelin is an extracellular glycoprotein essential for neuronal migration, spine development, and synaptic plasticity. Impaired reelin signaling is linked to neurological disorders, including schizophrenia and autism. While reelin mutant (reeler) mice exhibit behavioral deficits associated with impaired spine formation, the underlying molecular mechanisms remain unclear. We identified Twinfilin-1 (Twf1) as a downstream effector of reelin signaling via phosphoproteomic analysis, based on its reduced tyrosine phosphorylation in reeler mice. We found that Src regulated Twf1 phosphorylation at tyrosine 309, and reelin stimulation increased Twf1 phosphorylation in neurons, an effect blocked by the Src inhibitor PP2. A phospho-resistant Twf1 mutant (Twf1 Y309F) showed reduced capping protein binding and a lower F/G-actin ratio. Twf1 mice exhibited cognitive deficits, reduced spine density, smaller spine head size, and a decreased F/G-actin ratio in synaptosomes. These findings highlight Twf1 phosphorylation as a key component of reelin signaling involved in actin remodeling and spine development. - Source: PubMed
Publication date: 2025/10/10
Dong GeyaoMori DaisukeMatsuzaki TetsuoTanaka RinakoItoh NorimichiMatsui TakaakiSato AyatoArioka YukoOkumura HirokiFukaya RyotaKuba HiroshiNagai TakuNabeshima ToshitakaIkesue HiroakiKohno TakaoHattori MitsuharuKaibuchi KozoOzaki NorioMizoguchi HiroyukiYamada Kiyofumi