FADD (Phospho-Ser191) Antibody
- Known as:
- FADD (Phospho-Ser191) Antibody
- Catalog number:
- 11820
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- FADD (Phospho-Ser191) Antibody
Related genes to: FADD (Phospho-Ser191) Antibody
- Gene:
- FADD NIH gene
- Name:
- Fas associated via death domain
- Previous symbol:
- -
- Synonyms:
- MORT1, GIG3
- Chromosome:
- 11q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-07
- Date modifiied:
- 2019-04-23
Related products to: FADD (Phospho-Ser191) Antibody
Related articles to: FADD (Phospho-Ser191) Antibody
- TNF can activate both prosurvival and prodeath signaling downstream of tumor necrosis factor receptor 1 (TNFR1). Survival signaling originates from TNFR1-containing membrane-bound complex I, while death signaling is driven by cytosolic complex II. Receptor-interacting protein kinase 1 (RIPK1) is a central component of both complexes but the molecular switch converting RIPK1 from a prosurvival scaffold in complex I to a prodeath kinase in complex II has remained elusive. Here, we identify the E3 ligase HERC4 as the molecular determinant of prodeath signaling. We show that HERC4 binds complex I-derived S166-phosphorylated, kinase-active RIPK1 and ubiquitinates it within its death domain. This enables RIPK1 oligomerization and assembly of the apoptosis-inducing RIPK1-FADD-caspase 8-containing complex IIa and, upon caspase inhibition, formation of the necroptosis-initiating RIPK1-RIPK3-containing necrosome. HERC4 deficiency protects mice from TNF-induced systemic inflammatory response syndrome and acute liver injury. Thus, HERC4 is the link enabling complex I-derived RIPK1 to initiate death signaling. - Source: PubMed
Publication date: 2026/09/28
Lu HaohaoDu TongdeLi LinCao DongmeiLi KeLiu LinjieLi RuiYu XiaoliangHou ShouqiaoWang XinhuiShi MinyanLiu YanfenMa FengChen SheWalczak HenningHe Sudan - The RAS-MAPK pathway is frequently dysregulated in cancer, leading to malignant transformation. We previously identified a direct interaction between MyD88, a central adaptor of inflammatory signaling, and ERK, the terminal kinase of the RAS-MAPK cascade. Pharmacologic disruption of this ERK-MyD88 complex with a small molecule induces immunogenic cell death and antitumor immunity, suggesting a novel therapeutic strategy. Here, we show that ERK-MyD88 inhibition drives cellular signaling from non-canonical hubs. First, ERK-MyD88 disruption activates an integrated stress response that drives caspase-8-dependent apoptosis through a FADD-independent pathway within p62-ubiquitin aggregates. Second, it promotes assembly of MyD88, IRAK1, and IRAK4 into Myddosomes that produce proinflammatory chemokines independently of TLR or IL-1R activation. These findings demonstrate that perturbation of the ERK-MyD88 complex rewires cellular signaling into cell-autonomous hubs that coordinate caspase activation with chemokine secretion, thereby driving a program of immunogenic cancer cell death. - Source: PubMed
Publication date: 2026/07/30
Hussein NaderSkafi NajwaPham Thuy HaGautier MelinaVirard FrancoisFauvet FrédériqueMagadoux LéaChassot-Lamblot ChristelleMorel Anne-PierreVanbelle ChristopheBadran BassamLebecque SergeManié Serge NicolasLamure SylvainRenno TouficCoste Isabelle - As a fundamental life process, the cell cycle supports organismal development and genetic material stability. Phosphorylation is the principal molecular mechanism whereby the cyclin-dependent kinase (CDK)-cyclin complex triggers and regulates key events of the cell cycle, ensuring the temporally ordered progression of the cycle. Herein, FAS-associated death domain (FADD) (BmFADD) was identified as a phosphorylation-dependent cell cycle regulator. We demonstrated that BmCDK2 phosphorylates BmFADD at serine 130 (Ser130), preventing its lysosomal-autophagic degradation and promoting a specific interaction (amino acids 69 to 135). This interaction drives the nuclear translocation of BmFADD and acts as a competitive regulator of BmCyclinA-BmCDK2 binding to prevent premature S-phase exit. Furthermore, we generated a transgenic silkworm strain with silk-gland-specific knockout of the gene and found that loss of BmFADD activated mTOR, promoting endoreplication in silk gland cells and enhancing silk yield. Collectively, our results revealed a phosphorylation-dependent regulatory axis in which BmCDK2-mediated BmFADD phosphorylation at Ser130 competes against BmCyclinA that orchestrates S-phase progression. We confirmed that BmFADD modulates endoreplication through the mTOR signaling pathway. These findings expand the role of FADD in invertebrates, provide novel insights into posttranslational cell cycle regulation, and identify molecular targets for genetically engineering silkworm silk glands. - Source: PubMed
Publication date: 2026/09/22
Wang Lan-XingLong Yan-BiWei Si-YiZhang Ming-LiJia Xin-YueDong Zhan-QiLu ChengChen PengPan Min-Hui - This study investigated how inflammatory cell death-associated regulators influence the prognosis of lung adenocarcinoma (LUAD) and elucidated their underlying mechanisms. - Source: PubMed
Yang YalunLiu DiMa Shengwei - Baicalin is an ingredient of Qinbai Qingfei concentrated pills that is first new traditional Chinese medicine proved by SFDA for the treatment of pneumonia in children. We aim to investigate the role of Baicalin in the treatment of by inhibiting the ADP-ribosyltransferase of the D1 structural domain in the sole toxin CARDS TX of to down-regulating the expression of G-protein-coupled receptor. - Source: PubMed
Publication date: 2026/09/11
Liqiao YinYi SunHaifeng ZhangHongfei MaXuelin GeShuang LiangPing WangJin ChenFang FangWeiming WangYanli MengGuixin Tang