CtBP1 (Phospho-Ser422) Antibody
- Known as:
- CtBP1 (Phospho-Ser422) Antibody
- Catalog number:
- 11796
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- CtBP1 (Phospho-Ser422) Antibody
Related genes to: CtBP1 (Phospho-Ser422) Antibody
- Gene:
- CTBP1 NIH gene
- Name:
- C-terminal binding protein 1
- Previous symbol:
- -
- Synonyms:
- BARS
- Chromosome:
- 4p16.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-22
- Date modifiied:
- 2016-10-05
Related products to: CtBP1 (Phospho-Ser422) Antibody
Related articles to: CtBP1 (Phospho-Ser422) Antibody
- Abdominal aortic aneurysm (AAA) is a progressive vascular disease characterized by chronic inflammation and extracellular matrix (ECM) degradation. Although C-terminal binding protein 1 and 2 (CtBP1/2)-mediated transcriptional activation has been implicated in AAA progression, the upstream mechanisms regulating CtBP stability remain unclear. - Source: PubMed
Publication date: 2026/08/20
Bai LeiGe LijuanJiang BoSong Yanyan - The transcription factor ZEB2 has been implicated in cardiovascular disease, but its role and post-translational regulation in cardiac fibroblast-to-myofibroblast transition (FMT) and fibrosis after myocardial infarction (MI) are not fully understood. ZEB2 protein expression was significantly increased in infarcted murine hearts, activated cardiac fibroblasts, and human fibrotic myocardium. Myofibroblast-specific ZEB2 knockout alleviates cardiac dysfunction and adverse remodeling post-MI. Mechanistically, SENP1 regulated SUMO-1 modification of ZEB2 at K462, K479, K611, and K774. Reconstituting ZEB2-deficient systems with wild-type ZEB2 (ZEB2-WT) restored pathological fibrosis and FMT, whereas the SUMOylation-deficient mutant (ZEB2-4KR) conferred cardioprotective effects. ZEB2 SUMOylation activated the pro-fibrotic PI3K/AKT-mTORC1 signaling pathway. ZEB2-4KR weakens CtBP1 binding and enhances ZEB2 occupancy at the Nr4a1 promoter. Importantly, Nr4a1 knockdown abolished the protective effects of ZEB2-4KR. These findings identify SUMO-1 modification of ZEB2 as a central driver and molecular switch of pathological cardiac remodeling after MI and suggest that targeting ZEB2 SUMOylation may represent a promising therapeutic strategy. - Source: PubMed
Publication date: 2026/08/06
Wang YilinCheng ShaopengChen HongyuYang ZhihaoWu XiaotingZong QiuyanWang JianingJiang YiYu YanrongChen HaoXue YunxingZhao QianwenYang JieWang Dongjin - Hypotonia, Ataxia, Developmental Delay, and Tooth Enamel Defect Syndrome (HADDTS; OMIM #617915) is an ultra-rare autosomal dominant disorder caused by predominantly de novo pathogenic variants in , encoding a NAD(H)-dependent transcriptional corepressor. We reviewed all HADDTS cases reported from database inception to July 2026, searching PubMed/MEDLINE, Google Scholar, ClinVar, DECIPHER, OMIM, preprint servers, and the HADDTS Foundation, identifying 25 peer-reviewed cases from at least 11 countries; registries indicate at least 50 known individuals. Global developmental delay and language impairment were universal (25/25, 100%), followed by intellectual disability (24/25, 96%), hypotonia (22/25, 88%), ataxia and enamel defects (19/25, 76% each), cerebellar atrophy (18/25, 72%), feeding difficulties (15/25, 60%), myopathy (15/25, 60%), regression (10/25, 40%), oculomotor apraxia (7/25, 28%), scoliosis (6/25, 24%), respiratory chain dysfunction (5/25, 20%), skeletal anomalies (4/25, 16%), and seizures (2/25, 8%). The recurrent p.Arg342Trp (NM_001328.2; p.Arg331Trp, MANE Select NM_001012614.2) accounts for 84%, with severity from mild impairment to profound disability. In all four non-recurrent-variant carriers the canonical tetrad was incomplete; seizures and classifying skeletal anomalies occurred only in that group. Mutant CTBP1 acts dominant-negatively and heterodimerises with the essential paralog CTBP2, explaining the multisystem severity. HADDTS is a neurodevelopmental-mitochondrial overlap disorder; registries, mitochondrial evaluation, and allele-specific therapies are priorities. - Source: PubMed
Publication date: 2026/08/06
Akdaş Enes YağızLu DingyuZhang LinshenCheng MingzhenBashiri Dezfouli AliWollenberg Barbara - After fertilization, maternally deposited mRNAs are cleared, and de novo transcription is initiated through zygotic genome activation (ZGA), a core event of the maternal-to-zygotic transition in mice. 2-cell-like cells (2CLCs), a rare MERVL-positive subpopulation of mouse embryonic stem cells, partially recapitulate transcriptional features of 2-cell embryos. Although canonical MERVL-high 2CLCs depend on DUX, Dux knockout embryos can develop to term, suggesting that 2CLC models do not fully capture DUX-independent pathways associated with preimplantation transcriptional programs. Here, we show that disruption of C-terminal binding protein 1/2 (Ctbp1/2) activates both DUX-dependent minor ZGA-associated genes and DUX-independent major ZGA- and post-ZGA-associated programs. Pramel7 is derepressed independently of DUX and contributes to subsets of both programs. PRAMEL7 overexpression partially rescues transcriptional defects caused by Dux deletion and is associated with UHRF1 downregulation and DNA demethylation-linked activation of post-ZGA-associated genes. These findings identify CtBP1/2 as repressors of multiple early embryonic transcriptional programs in mouse embryonic stem cells. - Source: PubMed
Publication date: 2026/08/03
Yoshioka KazumaIchisakino MakiSugiyama KotaHayakawa NaoAbadi Selma AlamandaYoon HeekyoungMarutani MiyuMasuda RyoTakahashi KyoSeki Yoshiyuki - Non-small cell lung cancer (NSCLC) remains a leading cause of global cancer mortality. Increasing evidence implicates aberrant cholesterol metabolic reprogramming as a key facilitator of tumour malignancy; however, the mechanistic connections between lipoprotein metabolism and NSCLC pathogenesis remain elusive. Here, we investigate the unrecognised oncogenic role of cholesteryl ester transfer protein (CETP), a central lipid exchange mediator. - Source: PubMed
Chen YanjieWang HengTan XiminYan ChenxiLiu FangfangDeng ShuxuanWang ChengyanXia YangchenXu ZhaolinWu KongmingHuang ShanshanChu Qian