SQSTM1 Antibody (Center S207) Blocking Peptide
- Known as:
- SQSTM1 Antibody (Center S207) Blocking Peptide
- Catalog number:
- BP19360c
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SQSTM1 Antibody (Center S207) Blocking Peptide
Related genes to: SQSTM1 Antibody (Center S207) Blocking Peptide
- Gene:
- RNA5SP207 NIH gene
- Name:
- RNA, 5S ribosomal pseudogene 207
- Previous symbol:
- RN5S207
- Synonyms:
- -
- Chromosome:
- 6p21.1
- Locus Type:
- pseudogene
- Date approved:
- 2011-11-04
- Date modifiied:
- 2014-11-19
- Gene:
- SQSTM1 NIH gene
- Name:
- sequestosome 1
- Previous symbol:
- PDB3, OSIL
- Synonyms:
- p62, p60, p62B, A170
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-13
- Date modifiied:
- 2019-03-07
Related products to: SQSTM1 Antibody (Center S207) Blocking Peptide
Related articles to: SQSTM1 Antibody (Center S207) Blocking Peptide
- Ferroptosis is an iron-dependent form of regulated cell death driven by lipid peroxidation; however, how selective autophagy regulates ferroptotic sensitivity remains incompletely understood. Here, we identify RAB8A as a selective autophagic substrate and negative regulator of ferroptosis. Quantitative proteomic analyses reveal that ferroptotic stress induces ATG5- and ATG7-dependent degradation of RAB8A. Mechanistically, ferroptotic stimuli induce RNF126-dependent polyubiquitination of RAB8A and subsequent SQSTM1-mediated autophagic degradation. Functionally, loss of sensitizes cancer cells to ferroptosis, whereas expression of the degradation-resistant active mutant RAB8A suppresses ferroptotic cell death. RAB8A interacts with TFRC and facilitates stress-induced redistribution of TFRC from the plasma membrane toward endolysosomal compartments. deficiency impairs TFRC clearance, enhances transferrin-dependent iron uptake, and increases intracellular Fe accumulation and lipid peroxidation. In fibrosarcoma and pancreatic cancer xenograft models, depletion enhances the antitumor efficacy of ferroptosis-inducing therapy. Clinically, RAB8A is upregulated and associated with poor prognosis and ferroptosis resistance in pancreatic cancer. Collectively, these findings establish an autophagy-RAB8A-TFRC axis that regulates ferroptotic sensitivity. - Source: PubMed
Publication date: 2026/08/30
Li JingboZhou QileLiu JiaoChen XinYu ChunhuaKang RuiTang Daolin - Unconventional TCRαβ CD4CD8 double negative T cells (DNT) can effectively impede the progression of leukemia, lymphoma, and solid tumors, highlighting their potential as a novel and effective cell therapy approach for cancer. However, the intrinsic mechanisms regulating DNT homeostasis and anti-tumor functions remain unclear. In this study, we discovered that DNT highly expressed IFITM1 (interferon-induced transmembrane protein 1) and further demonstrated that IFITM1 actively regulated the anti-tumor function of DNT both in vitro and in vivo. Furthermore, our investigation revealed that IFITM1 DNT exhibited elevated expression of key molecules involved in immune cell-mediated anti-tumor responses, such as perforin, granzyme B, and NKG2D. Overexpression of IFITM1 promoted DNT anti-tumor activity. Notably, IFITM1 regulated mitophagy, which contributed to the improved mitochondrial function in DNT. Mechanistically, IFITM1 in the mitochondria of DNT interacts with the autophagosomal cargo protein p62/SQSTM1, recruiting more p62/SQSTM1 to the mitochondria, thereby promoting mitophagy. It is worth noting that IFITM1 is also highly expressed in activated human DNT (hDNT), and its regulatory effect on DNT mitophagy, homeostasis, and anti-tumor function has been validated. In conclusion, IFITM1 has emerged as a crucial player in enhancing DNT-mediated anti-tumor activity by regulating mitophagy and mitochondrial function. These findings suggested that upregulating IFITM1 expression in DNT may enhance mitophagy and promote DNT survival and cytotoxic functions, ultimately providing better control over cancer. - Source: PubMed
Publication date: 2026/08/26
Han XiaotongDu XiaonanZhou LongyangZhang ZihanZhu JingjingWang XiyuJiang YuanSun JieTian YueWang SonglinZhang ZhongtaoSun GuangyongZhang Dong - Connexin 36 (Cx36), a neuronal gap junction protein, is essential for retinal signal transmission but may also contribute to neurodegeneration by facilitating the spread of excitotoxic stress signals. This study aimed to examine the degradation pathway of Cx36 under stress conditions relevant to retinal disease. Using immortalized 661W murine photoreceptor cells transfected with GFP-tagged Cx36, we evaluated the effects of lysosomal inhibition (Bafilomycin A1) and excitotoxic stimulation (NMDA). Immunofluorescence revealed intracellular Cx36 accumulation following Bafilomycin and NMDA exposure, accompanied by increased expression of p62/SQSTM1 and PSMA1, suggesting impaired autophagic flux and a potential compensatory involvement of the proteasome. Elevated RAB11A levels suggested recruitment of endosomal recycling pathways. NMDA treatment was associated with increased ubiquitin accumulation, particularly in Cx36-overexpressing cells, indicating enhanced proteostatic stress under excitotoxic conditions. These findings highlight the stress-responsive behavior of Cx36 and suggest that connexin proteostasis may represent a potential target for future investigation in retinal neurodegeneration, including glaucoma and age-related macular degeneration. Immunofluorescence revealed intracellular accumulation of p62 and PSMA1 after Bafilomycin exposure with signal intensities increasing approximately 1.5-2-fold versus controls (n = 3, p < 0.05). These data are consistent with disrupted autophagic flux and suggest proteasome involvement, but do not constitute functional proof. - Source: PubMed
Publication date: 2026/08/14
Katan MonikaMróz KlaudiaPacwa AnnaLewin-Kowalik JoannaSmędowski Adrian - RNA viruses, major pathogens of humans and animals, are responsible for numerous inflammatory diseases. Commonly, mild RNA virus infection fails to trigger inflammatory diseases due to host immune homeostasis. However, severe RNA virus infection destroys immune homeostasis and causes hyperinflammation. The detail mechanism is still unclear. Here, we reported that SESN1 acts as a critical negative regulator of mitochondrial antiviral signaling protein (MAVS), a central hub protein in RNA-triggered innate immune response, by potentiating MAVS autophagic degradation to repress innate immune response. Upon low dose RNA virus infection, SESN1 level was decreased at infection early stage and was rebounded at late stage, which restrained SESN1-mediated MAVS degradation to clear virus at early stage and enhanced MAVS degradation to prevent excessive cytokines production at late stage. Whereas, SESN1 level was continuously impaired after high dose RNA virus infection, which caused robust cytokines production. Notably, we observed that the expression of SESN1 was markedly downregulated and negatively correlated with cytokine levels in patients with severe influenza. Replenishment of SESN1 effectively inhibited cytokines production in the Human Primary Bronchial/Tracheal Epithelial Cells infected with Influenza A virus PR8 and peripheral blood mononuclear cells of patients with severe influenza. Mechanistically, SESN1 interacted with MAVS and enhanced MAVS autophagic degradation via SQSTM1. Together, these findings revealed SESN1 was an important factor to regulate host innate immune response. - Source: PubMed
Publication date: 2026/08/26
Liu QianghuiChen PeiranHe ChunyanQiu ZuochengZhang YuboWang JiaXu LingxiaoXu YongPan Mingyu - Triple-negative breast cancer (TNBC), characterized by aggressive behavior and poor prognosis, presents a formidable clinical challenge. Despite guideline endorsement of chemoimmunotherapy as a standard treatment in TNBC, durable responses remain rare, largely due to an immunologically "cold" tumor microenvironment (TME). Through integrated analysis, we identified the F-box protein FBXW5 as a tumor-intrinsic immunosuppressive regulator, whose expression is elevated in immunologically "cold" TNBC and correlates with dismal patient survival. Genetic knockdown of murine Fbxw5 suppressed tumor growth, reinvigorated CD8+ T cell-mediated antitumor immunity, and sensitized TNBC tumors to both single-agent and combined chemo-immune therapy in preclinical models. Mechanistically, FBXW5 acts within the SKP1/CUL1/F-box protein (SCF) E3 ligase complex to bind RIGI and MDA5, promoting their K27-linked polyubiquitination and subsequent SQSTM1-mediated autophagic degradation. This process blunts cytosolic RNA sensing and type I interferon (IFN-I) signaling, thereby limiting CD8+ T cell infiltration and activation. Our findings establish FBXW5 as a master regulator of the "cold" TME, presenting a potential predictive biomarker and actionable therapeutic target for enhancing chemoimmunotherapy in TNBC. - Source: PubMed
Publication date: 2026/08/25
Li XinChen TongZhao WenjingLi JiaxingShang YifanChen BingWang LijuanZhang NingKong XiaoliLiang YiranLi YamingLi ChenHan DianwenChen XiJiang ShanYang ChaoLuo DanMa TingtingYang Qifeng