SQSTM1 Antibody (N-term S24)
- Known as:
- SQSTM1 Antibody (N-terminus S24)
- Catalog number:
- AP19120a-ev20
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SQSTM1 Antibody (N-term S24)
Related genes to: SQSTM1 Antibody (N-term S24)
- Gene:
- CHMP3 NIH gene
- Name:
- charged multivesicular body protein 3
- Previous symbol:
- VPS24
- Synonyms:
- NEDF, CGI-149
- Chromosome:
- 2p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-11
- Date modifiied:
- 2014-11-19
- Gene:
- HSPA4 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 4
- Previous symbol:
- -
- Synonyms:
- HS24/P52, HSPH2
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2015-11-19
- Gene:
- KLRK1 NIH gene
- Name:
- killer cell lectin like receptor K1
- Previous symbol:
- D12S2489E
- Synonyms:
- NKG2D, KLR, NKG2-D, CD314
- Chromosome:
- 12p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-12
- Date modifiied:
- 2016-10-05
- Gene:
- MRPS24 NIH gene
- Name:
- mitochondrial ribosomal protein S24
- Previous symbol:
- -
- Synonyms:
- MRP-S24, HSPC335
- Chromosome:
- 7p13
- Locus Type:
- gene with protein product
- Date approved:
- 2001-01-26
- Date modifiied:
- 2016-10-05
- Gene:
- RNA5SP24 NIH gene
- Name:
- RNA, 5S ribosomal pseudogene 24
- Previous symbol:
- RN5S24
- Synonyms:
- -
- Chromosome:
- 13q12.11
- Locus Type:
- pseudogene
- Date approved:
- 2011-08-08
- Date modifiied:
- 2012-08-07
Related products to: SQSTM1 Antibody (N-term S24)
Related articles to: SQSTM1 Antibody (N-term S24)
- Atherosclerosis is a chronic vascular disease characterized by the accumulation of lipid-filled foam cells in the arterial wall. Macrophage-derived foam cells play a key role in promoting plaque formation. α-Tocopherol (α-TOC), a common dietary antioxidant, is thought to have protective effects against atherosclerosis, but its specific mechanisms remain unclear. In this study, an foam cell model was established using oxidized low-density lipoprotein-induced macrophages to investigate the effects of α-TOC on foam cell formation and related mechanisms. Network pharmacology predicted that α-TOC may act through autophagy-related pathways, particularly the mTOR-mediated autophagy pathway. We demonstrated that α-TOC enhanced autophagic function in macrophages, as evidenced by increased expression of Beclin1, LC3-II, ATG5, and ATG12, along with reduced p62/SQSTM1 levels. Rapamycin reproduced, and 3-methyladenine opposed, the direction of the autophagic and mTOR/ULK1 changes observed with α-TOC, consistent with involvement of this pathway. These findings suggest that α-TOC reduces lipid accumulation and inhibits foam cell formation in macrophages by enhancing autophagic activity in association with reduced mTOR phosphorylation and increased ULK1 Ser555 phosphorylation. This study provides mechanistic insights into the potential anti-atherosclerotic effects of α-TOC at the cellular level, offering a theoretical basis for its further investigation as a therapeutic candidate for atherosclerosis. - Source: PubMed
Publication date: 2026/09/16
Kuang LuWu LimeiLiu ZenghuiZhao JiaxingChen QijunYin HuayuLiu XuehuiLiu DabinWu Shaoguo - Quality control of biomolecules is vital for organismal health. While DNA repair and protein quality control are well understood, how cells monitor other important biomolecules such as glycogen remains ill-defined. The accumulation of aberrant, poorly branched glycogen into insoluble polyglucosan bodies causes severe disease. Here, we discover autophagy of ubiquitylated aberrant glycogen as a previously unrecognized quality control mechanism safeguarding the brain from polyglucosan buildup. This mechanism depends on the E3 ubiquitin ligase RNF213. Mice lacking ligase activity in RNF213 accumulate polyglucosan in cerebellum, pons, and hippocampus. Using cells engineered to produce polyglucosan, we show that RNF213 selectively ubiquitylates abnormal glycogen. Cryo-EM analysis of RNF213 bound to glycogen-derived maltoheptaose revealed its CBM20 domain binds linear oligosaccharides. Disrupting carbohydrate binding results in gain of E3 ligase activity towards physiological glycogen, indicating the CBM20 domain limits RNF213 activity towards physiological glycogen. Epistasis analysis places RNF213 upstream of LUBAC, suggesting a hierarchical network of multiple E3 ligases surveying glycogen quality. Ubiquitylated polyglucosan recruits the autophagy receptors SQSTM1, TAX1BP1, and optineurin, thereby triggering uptake into autophagosomes. These findings identify RNF213 as a quality control factor preventing polyglucosan accumulation in astrocytes through direct ubiquitylation of polyglucosan, revealing an essential role for non-protein ubiquitylation in glycogen quality control. - Source: PubMed
Publication date: 2026/09/15
Yip Matthew C JNaydenova KaterinaOtten Elsje GHeatley AlexanderMoe AgnesAnton Leoniede Los Reyes-Ramírez LucíaJolin Helen ELangevin FredericWiacek MichalFranco CatarinaBertolotti AnneKukulski WandaMcKenzie Andrew N JRandow Felix - Porcine reproductive and respiratory syndrome virus (PRRSV) is one of the most devastating pathogens affecting the global swine industry. Autophagy plays an important role in both host defense and PRRSV infection. However, the mechanisms by which the host exploits the autophagy pathway to antagonize PRRSV infection remain largely unknown. Here, we perform transcriptomic analysis of porcine alveolar macrophages isolated from PRRSV-infected piglets and reveal a significant upregulation of the mRNA levels for the E3 ubiquitin ligase IDOL. These findings are further validated by experiments. Functional studies reveal that IDOL acts as a host restriction factor for PRRSV: ectopic expression of IDOL markedly suppresses viral replication, while knockdown of endogenous IDOL enhances it. Mechanistically, IDOL catalyzes K63-linked polyubiquitination of the viral nonstructural protein 3 (Nsp3) at lysine 101 (K101) and recruits the selective autophagy receptor SQSTM1, thereby targeting Nsp3 for degradation via the autophagy-lysosomal pathway and effectively suppressing viral replication. Notably, the ubiquitin-associated and LC3-interacting region domains of SQSTM1 are essential for this autophagic clearance of Nsp3. Furthermore, using a reverse genetics approach, we generate an Nsp3 K101R mutant virus and confirm that this specific mutation enables the virus to evade IDOL-mediated Nsp3 degradation, thereby restoring its replication competence. In summary, we uncover an autophagy-dependent antiviral mechanism, establish IDOL as an innate immune regulator with a non-canonical function, and define a viral immune evasion strategy, positioning IDOL as a promising therapeutic target for PRRSV control.IMPORTANCEPorcine reproductive and respiratory syndrome virus (PRRSV) represents a major threat to global swine production, inflicting substantial economic damage and endangering food security. Here, we identify the E3 ubiquitin ligase IDOL as a critical host restriction factor that combats PRRSV through a previously unrecognized autophagy-mediated mechanism. We demonstrate that PRRSV infection robustly upregulates the transcription factor ZNF460, which directly drives IDOL expression. During PRRSV infection, IDOL drives the autophagic degradation of Nsp3 by catalyzing its K63-linked ubiquitination at lysine 101 and engaging the selective autophagy receptor SQSTM1, triggering a potent antiviral response. Using reverse genetics, we generate an Nsp3 K101R mutant virus and demonstrate that this mutation enables the virus to escape IDOL-mediated degradation and restore replication competence, providing genetic validation of this antiviral axis. Collectively, our findings establish an autophagy-dependent antiviral mechanism, define IDOL as an intrinsic immune regulator with a previously unrecognized function, and elucidate a precise viral immune evasion strategy, thereby positioning IDOL as a promising therapeutic target for PRRSV intervention. - Source: PubMed
Publication date: 2026/09/15
Yan JiecongWu YuhanXu HuiruiLai PengningHuang LingHe ZhanXie YongshengGuo Chunhe - Pancreatic ductal adenocarcinoma (PDAC) is an aggressive malignancy characterized by poor prognosis and limited response to gemcitabine, the standard first-line chemotherapy. One major contributor to chemoresistance is autophagy, a process frequently upregulated in PDAC. In this study, we examined the ability of type I interferons (IFNα2b and IFNβ1a) to modulate autophagy and disturb tumor cell resistance to gemcitabine. PDAC cells were treated with increasing concentrations of IFNα2b or IFNβ1a, and cell proliferation was assessed by [H]-thymidine incorporation. Apoptosis was evaluated by TUNEL staining following treatments with interferons and/or gemcitabine. STAT1 phosphorylation was analyzed as a marker of downstream type I interferon signaling. Autophagy was analyzed by western blot for LC3B, Beclin-1, Bcl-XL and p62/SQSTM1, and by quantifying autophagic flux using mCherry-EGFP-LC3B-transfected cells in the presence or absence of lysosomal inhibitors. We found that IFNα2b promoted autophagic flux and reduced gemcitabine-induced cell death, indicating a cytoprotective role. In contrast, IFNβ1a reduced autophagosome formation and significantly enhanced cell death, without clear evidence of altering autophagic flux. Both interferons induced STAT1 phosphorylation, confirming engagement of downstream type I interferon signaling. Our findings highlight the contrasting roles of IFNα2b and IFNβ1a in the regulation of autophagy and gemcitabine response and suggest that IFNβ1a, by reducing autophagosome formation, may sensitize PDAC cells to chemotherapy. These findings identify IFNβ1a as a potential chemosensitizing agent in PDAC and provide a rationale for further evaluating combinations of IFNβ1a, gemcitabine, and autophagy-targeting strategies to overcome chemoresistance. - Source: PubMed
Publication date: 2026/09/15
Bonilla Lucy ELedesma Martín MBehr Santiago APibuel Matías APalanek María LGrasso Daniel HGarcia Maria NGarona JuanLompardía Silvina LÁlvarez ElidaPapademetrio Daniela L - Persistently poor glioblastoma (GBM) survival necessitates better elucidation of tumor drug responses. After observing that low curcumin and all-trans retinoic acid (ATRA) doses stimulated cell proliferation and counteracted each other's high-dose antiproliferative effects in U87 GBM cells, drug influences on cell growth, migration, and death and the antiproliferative interaction proteome were further studied. Cell proliferation and migration were assessed by xCELLigence Real-Time Cell Analysis (RTCA). Cell death was defined using flow cytometry. Drug interactions were determined with CompuSyn software (version 1.0). Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS), High-Performance Liquid Chromatography (HPLC), and SequestHT software (version 1.4) were utilized for peptide generation and identification. ATRA at high doses inhibited cell growth and migration more efficiently. Curcumin was more proliferative and antagonistic against anti-growth effects at low doses. Migration inhibition and apoptosis occurred synergistically at the highest drug doses. ATRA influenced the proteome more remarkably, reducing Transforming Growth Factor Beta Induced (TGFBI), Phosphoglycerate Dehydrogenase (PHGDH), tenascin, and Sequestosome 1 (SQSTM1). These effects were alleviated by curcumin, except for SQSTM1. Uveal Autoantigen With Coiled-Coil Domains And Ankyrin Repeats (UACA) and Sad1 And UNC84 Domain Containing 2 (SUN2) were increased by ATRA and curcumin, and to a lesser extent by the combination. Hexokinase 2 (HXK2) was increased by curcumin and the combination. Heme Oxygenase 1 (HMOX1) was depleted by the combination, but not by the single agents. SQSTM1 and HMOX1 reductions may mediate anticancer synergism, while the remaining changes may indicate ongoing hormetic pathways not reflected in cell counts. - Source: PubMed
Publication date: 2026/08/31
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