ATG13 Polyclonal Antibody Autophagy Antibody
- Known as:
- ATG13 Polyclonal Antibody Autophagy Antibody
- Catalog number:
- AUT-5799
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- ATG13 Polyclonal Antibody Autophagy
Related genes to: ATG13 Polyclonal Antibody Autophagy Antibody
- Gene:
- ATG13 NIH gene
- Name:
- autophagy related 13
- Previous symbol:
- KIAA0652
- Synonyms:
- -
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-10-28
- Date modifiied:
- 2014-11-19
Related products to: ATG13 Polyclonal Antibody Autophagy Antibody
Related articles to: ATG13 Polyclonal Antibody Autophagy Antibody
- Esophageal cancer (EC) remains an extremely lethal cancer with few prognostic biomarkers and specific therapies. Although autophagy is increasingly recognized as a key force behind tumor adaptation and resistance to therapy, its systematic role at the EC progression level for prognostics, as well as for drug target prediction, remains unclear. Here, we attempted to build a systems-wide map linking autophagy- and signaling-related genes and transcriptional dysregulation, patient survival, and druggability in EC. Hub genes were found using an integrative bioinformatics pipeline based on protein-protein interaction networks and further explored using enrichment, expression, survival, and molecular docking analyses. Functional enrichment highlighted autophagy, mitophagy, ferroptosis, and immune signaling as central processes, converging with stress- and metabolism-associated pathways. Expression profile of TCGA-ESCA data demonstrated substantial overexpression of autophagy initiators and elongation factors (ATG3, ATG5, ATG7, ATG12, ATG13), upstream regulators (AMBRA1, UVRAG), and stress/metabolic mediators (TP53, MYD88, GAPDH). Kaplan-Meier analysis indicated three genes, including ATG4A, GABARAPL2, and GAPDH, that exhibited significant expression levels correlating with less survival and emphasizing their prognostic capacities. Screening for drugs also revealed AKT1, TP53, and PIK3R4 as druggable hubs, and many drugs (e.g., Everolimus, Dabrafenib, Trabectedin) showing high-affinity interactions. These findings collectively demonstrate that the progression of EC is supported by a coordinated program that integrates autophagy and metabolic reprogramming with stress and immunological signaling. The study discovers new prognostic markers (ATG4A, GABARAPL2, GAPDH) and druggable targets, which could lead to better risk stratification and smarter drug repurposing. While restricted to in silico analyses, the integrative approach provides a basis for subsequent laboratory confirmation and translational development. - Source: PubMed
Publication date: 2026/05/27
Salehi ShirinMottaghi-Dastjerdi NegarShahbazi BehzadAhmadi NahidGhorbani AbozarSoltany-Rezaee-Rad MohammadYazdani FatemeKhoshdel FarzaneNiazi Mohammad-Javad - The term CASM describes a process in which MAP1LC3B/LC3B and other Atg8-family proteins are covalently ligated to lipids in damaged endomembranes. While CASM is commonly described as a cytoprotective response to multiple types of membrane damage, how CASM helps cells maintain homeostasis is still unclear. Here, we show that CASM maintains Golgi apparatus architecture following the loss of TRIM46, a ubiquitin ligase with roles in microtubule organization. TRIM46 deficient cells were notable for enhanced TFEB-driven lysosomal biogenesis and Golgi ribbon fragmentation, with colocalization of the -Golgi marker TGOLN2 and the Atg8-family proteins LC3B and GABARAP. Further studies revealed that the Golgi Atg8ylation seen in knockout cells was not degradative and mechanistically resembled CASM. Genetic inhibition of CASM in TRIM46 deficient cells reduced TFEB activation and exacerbated the Golgi morphology defects, suggesting that CASM contributes to Golgi repair. Accordingly, Golgi reformation after drug-induced fragmentation was impaired upon knockdown of CASM genes. Together, these studies identify lysosomal biogenesis and CASM as coordinated features of a Golgi damage response, with CASM acting to preserve Golgi integrity. AMPK (AMP-activated protein kinase); ATG3 (autophagy related 3); ATG5 (autophagy related 5); ATG7 (autophagy related 7); ATG12 (autophagy related 12); ATG13 (autophagy related 13); ATG16L1 (autophagy related 16 like 1); BECN1 (beclin 1); CASM, conjugation of Atg8 to single membranes; GABARAP (GABA type A receptor-associated protein); GABARAPL1 (GABA type A receptor associated protein like 1); GABARAPL2 (GABA type A receptor associated protein like 2); GOLGA2 (golgin A2); HT (HaloTag); HL (HaloTag ligand); MAP1LC3A/LC3A (microtubule associated protein 1 light chain 3 alpha); MAP1LC3B/LC3B (microtubule associated protein 1 light chain 3 beta); MAP1LC3C/LC3C (microtubule associated protein 1 light chain 3 gamma); MTORC1 (mechanistic target of rapamycin kinase complex 1); PE (phosphatidylethanolamine); PIK3C3/VPS34 (phosphatidylinositol 3-kinase catalytic subunit type 3); PS (phosphatidylserine); TECPR1 (tectonin beta-propellor repeat containing 1); SQSTM1/p62 (sequestosome 1); TFEB (transcription factor EB); TFE3 (transcription factor binding to IGHM enhancer 3); TGOLN2 (trans-golgi network protein 2); TRIM46 (tripartite motif containing 46); ULK1 (unc-51 like autophagy activating kinase 1); ULK2 (unc-51 like autophagy activating kinase 2): VAIL (V-ATPase-ATG16L1 induced LC3 lipidation). - Source: PubMed
Publication date: 2026/05/18
Oh SeeunUllah SaifSaha BhaskarMandell Michael A - Ovarian cancer (OC) is often characterized by poor prognosis due to paclitaxel (TAX) resistance, with ferredoxin 1 (FDX1) emerging as a key mediator of copper metabolism. The present study aimed to elucidate the role of FDX1 in TAX resistance and to evaluate the efficacy of pH/reactive oxygen species (ROS)-responsive nanomicelles (PPD/PDP@si-FDX1) in reversing this resistance. - Source: PubMed
Publication date: 2026/04/23
Gong YangmeiDeng ZhizhiWu JieHu Yi - Mitophagy - the selective degradation of damaged mitochondria - preserves mitochondrial quality; yet, how mitochondrial fission is coordinated with autophagy initiation remains unclear. Here, we identified the mitochondrial outer membrane protein MTFR1L as a key component of mitophagy initiation hubs after using a synthetic FKBP-FRB system to tether ULK1 kinase to mitochondria independently of damage. We found that MTFR1L was enriched at ULK1 foci together with additional fission factors, and constitutive mitochondrial targeting of MTFR1L shifted mitochondrial morphology towards fragmentation. MTFR1L depletion decreased respiratory capacity, elevated apoptosis and impaired mitophagy flux. Upon mitophagy induction, MTFR1L was phosphorylated in a ULK1 kinase-dependent manner and reciprocally modulated ULK1 activity, establishing a feedback loop. Moreover, MTFR1L was required for proper ATG13 stability. These findings position MTFR1L as a critical link between mitochondrial fission and the autophagy machinery, coordinating mitophagy initiation and cell survival. - Source: PubMed
Publication date: 2026/05/11
Babic RiccardoLucya LeonReiter ChristophKriegenburg FranziskaCastellanos-MartÃnez RamónHollenstein David MBecker FlorianHunte CarolaKraft Claudine - Macroautophagy (hereafter autophagy) is a conserved intracellular degradation pathway that is essential for maintaining cellular homeostasis. Autophagosome formation involves preautophagosomal structure (PAS) organization and expansion of the isolation membrane (IM). Although phosphatidylinositol 4-phosphate (PtdIns4P) localizes to the IM and is required for autophagy, the specific functional role it plays in autophagosome formation remains unclear. Pik1, a PtdIns 4-kinase localized to the Golgi, plays a critical role in this process. We used temperature-sensitive pik1 mutant cells and found that PAS localization of autophagy-related Atg9, Atg17, Atg1, and Atg13 remained normal at the restrictive temperature, indicating that PAS scaffold formation was unaffected. In contrast, the recruitment of downstream Atg proteins, the PtdIns 3-kinase complex I, including Atg14, the Atg2-Atg18 complex, and Atg8, was impaired under the same condition. These findings demonstrate that Pik1-generated PtdIns4P is essential for PAS organization. Since Atg9 vesicles are derived from the Golgi, we hypothesized that PtdIns4P is transported to the PAS on Atg9 vesicles to mediate recruitment of downstream Atg proteins. To test this, we performed immunoprecipitation analysis using a PtdIns4P-binding protein and found that Atg9 was coimmunoprecipitated at the permissive temperature but not at the restrictive temperature. This result indicates that PtdIns4P is enriched on Atg9 vesicles through Pik1 activity. Moreover, our assessment in pik1 mutant cells showed that IM expansion is impaired at the restrictive temperature. Collectively, these results identify PtdIns4P as a key component of PAS organization. - Source: PubMed
Publication date: 2026/04/09
Lang HuichaoSuzuki Kuninori