Autophagy最新文献

{"title":"ATG9 inhibits <i>Rickettsia</i> binding to the host cell surface by blocking the rOmpB-XRCC6/KU70 interaction.","authors":"Chen Chen, Guoxu Liu, Kehan Xu, Aibao Chen, Ziyang Cheng, Xueping Yan, Ting Zhang, Yan Sun, Tian Yu, Jiayao Wang, Shuangshuang Luo, Weiting Zhou, Shengqun Deng, Yan Liu, Yanan Yang","doi":"10.1080/15548627.2025.2496363","DOIUrl":"10.1080/15548627.2025.2496363","url":null,"abstract":"<p><p>ickettsiae are tick-borne pathogens that infect human hosts through poorly characterized mechanisms. Herein, we report that ATG9 (autophagy related 9) plays a previously unrecognized role in inhibiting Rickettsia binding to the host cell surface. Unexpectedly, this new function of ATG9 is likely independent of macroautophagy/autophagy. Instead, ATG9 acts as a host defending factor by binding to XRCC6/KU70, a receptor of the Rickettsia outer-membrane protein rOmpB. Both ATG9 and rOmpB bind to the DNA-binding domain of XRCC6, suggesting a competitive role for ATG9 occupying the binding site of rOmpB to abrogate Rickettsia binding. Furthermore, we show that rapamycin transcriptionally activates ATG9 and inhibits rOmpB-mediated infection in a mouse model. Collectively, our study reveals a novel innate mechanism regulating Rickettsia infection and suggests that agonists of ATG9 May be useful for developing therapeutic strategies for the intervention of rickettsial diseases.<b>Abbreviation</b>: APEX2: apurinic/apyrimidinic endodeoxyribonuclease 2; ATG: autophagy related; BafA1: bafilomycin A1; CQ: chloroquine; E. coli: Escherichia coli; GST: glutathione S-transferase; ICM: immunofluorescence confocal microscopy; IP-Mass: immunoprecipitation-mass spectrometry; KD: knockdown; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MTOR: mechanistic target of rapamycin kinase; rOmpB: rickettsial outer membrane protein B; SAP: SAF-A/B, Acinus, and PIAS; SQSTM1/p62: sequestosome 1; TEM: transmission electron microscopy; TFEB: transcription factor EB; VWA: von Willebrand factor A; XRCC6/KU70: X-ray repair cross complementing 6.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2213-2229"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459360/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144031083","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ATG5 controls CD80 expression in B cells and shapes cognate CD4⁺ T cell responses.","authors":"Ingredy Passos, Thomas Zobel, Christian Münz, Anneli Peters, Jan D Lünemann","doi":"10.1080/15548627.2025.2507614","DOIUrl":"10.1080/15548627.2025.2507614","url":null,"abstract":"<p><p>The macroautophagy/autophagy machinery has been implicated in supporting MHC class II but compromising MHC class I restricted antigen presentation by dendritic cells (DCs). Here, we report that loss of the essential autophagy protein ATG5 in B cells reduces internalization and stabilizes co-stimulatory CD80 surface expression. In an adjuvant-free experimental autoimmune encephalomyelitis (EAE) mouse model, co-transfer of MOG-specific induced germinal center B (iGB) cells deficient in ATG5 with MOG-specific CD4⁺ T cells, accelerated disease development. CD80 blockade abrogated enhanced cognate CD4⁺ T-cell responses induced by iGB cells lacking ATG5. These data broaden the concept of ATG5-mediated antigen presentation and indicate that ATG5 might not only enhance, as described previously with MHC class II-restricted presentation in DCs, but also limit the activation of CD4⁺ T cells through attenuating CD80 expression on B cells.<b>Abbreviations</b>: APC: antigen-presenting cell; CNS: central nervous system; DC: dendritic cell; EAE: experimental autoimmune encephalomyelitis; iGB: induced germinal center B cell; MOG: myelin oligodendrocyte glycoprotein; MS: multiple sclerosis.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2284-2292"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459358/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144164301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MoSec13 combined with MoGcn5b modulates MoAtg8 acetylation and regulates autophagy in <i>Magnaporthe oryzae</i>.","authors":"Hui Qian, Ming-Hua Wu, Wen-Hui Zhao, Xue-Ming Zhu, Li-Xiao Sun, Jian-Ping Lu, Daniel J Klionsky, Fu-Cheng Lin, Xiao-Hong Liu","doi":"10.1080/15548627.2025.2499289","DOIUrl":"10.1080/15548627.2025.2499289","url":null,"abstract":"<p><p>Macroautophagy/autophagy is an evolutionarily conserved cellular degradation process that is crucial for cellular homeostasis in <i>Magnaporthe oryzae</i>. However, the precise regulatory mechanisms governing autophagy in this organism remain unclear. In this study, we found a multiregional localization of MoSec13 to the vesicle membrane, endoplasmic reticulum, nucleus, and perinucleus. MoSec13 negatively regulated autophagy through specific amino acid residues in its own WD40 structural domain by interacting with MoAtg7 and MoAtg8. We also found that the histone acetyltransferase MoGcn5b mediated the acetylation of MoAtg8 and regulated autophagy activity. Subsequently, we further determined that MoSec13 regulated the acetylation status of MoAtg8 by controlling the interaction between MoGcn5b and MoAtg8 in the nucleus. In addition, MoSec13 maintained lipid homeostasis by controlling TORC2 activity. This multilayered integration establishes MoSec13 as an essential node within the autophagic regulatory network. Our findings fill a critical gap in understanding the role of Sec13 in autophagy of filamentous fungi and provide a molecular foundation for developing new therapeutic strategies against rice blast fungus.<b>ABBREVIATIONS</b> BFA: brefeldin A; BiFC: bimolecular fluorescence complementation; CM: complete medium; CMAC: 7-amino-4-chloromethylcoumarin; Co-IP: co-immunoprecipitation; COPII: coat complex II; GFP: green fluorescent protein; HPH: hygromycin phosphotransferase; MM-N: nitrogen-starvation conditions; NPC: nuclear pore complex; PAS: phagophore assembly site; PE: phosphatidylethanolamine; UPR: unfolded protein response.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2266-2283"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459355/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144055275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction.","authors":"","doi":"10.1080/15548627.2024.2401222","DOIUrl":"10.1080/15548627.2024.2401222","url":null,"abstract":"","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"iv-xi"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459349/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142303282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction.","authors":"","doi":"10.1080/15548627.2025.2457111","DOIUrl":"10.1080/15548627.2025.2457111","url":null,"abstract":"","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"i-ii"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459352/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143392720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neutrophil-derived serine proteases induce FOXA2-mediated autophagy dysfunction and exacerbate colitis-associated carcinogenesis via protease activated receptor 2.","authors":"Junhu Yuan, Jianhui Ma, Fanyu Zhang, Tan Wang, Xiaxiang Jian, Bingzhi Wang, Weiwei Li, Xiaoli Zhang, Yubin Cao, Hong Yang, Yiming Ma, Hongying Wang","doi":"10.1080/15548627.2025.2489335","DOIUrl":"10.1080/15548627.2025.2489335","url":null,"abstract":"<p><p>Autophagy plays a critical role in colitis-associated colorectal cancer (CAC). However, non-autonomous regulation of macroautophagic/autophagic flux during inflammation remains largely unexplored. Here, we show that <i>F2rl1/Par2</i> deficiency (<i>F2rl1</i>[ΔIEC]) aggravated azoxymethane-dextran sulfate sodium-induced CAC based on tumor number and burden, promoted autophagy dysfunction characterized by SQSTM1/p62 accumulation and autophagosome-lysosome fusion inhibition in IECs, and reduced lysosomal acidification by suppressing FOXA2-induced V-ATPase <i>ATP6V0E1</i> transcription. <i>FOXA2</i> or <i>ATP6V0E1</i> overexpression rescued autophagy impairment, reactive oxygen species accumulation, and DNA damage induced by <i>F2RL1</i> deficiency <i>in vitro</i> and <i>in vivo</i>. Neutrophil-derived serine proteases suppressed <i>FOXA2</i> expression, causing autophagy dysfunction. <i>F2RL1</i> knockout completely blocked the effects of neutrophil proteases on <i>FOXA2</i> and <i>ATP6V0E1</i>. The correlation between neutrophil and <i>FOXA2-ATP6V0E1</i> activities was validated in ulcerative colitis and colorectal carcinoma. Therefore, <i>F2RL1</i> deficiency in intestinal epithelial cells suppressed <i>FOXA2</i> expression, leading to V-ATPase-mediated autophagic dysfunction and exacerbating CAC. Neutrophils may contribute to impaired autophagy and promote CAC by inactivating canonical F2RL1/PAR2 signaling via its derived proteases. F2RL1/PAR2 signaling may participate in maintaining intestinal homeostasis via autophagy. These findings provide useful insights into F2RL1/PAR2 and its cleaving serine proteases in CAC and would help in developing new therapeutic strategies for this malignancy.<b>Abbreviations</b>: AOM: azoxymethane; ATP6V0C: ATPase H+ transporting V0 subunit c; ATP6V0E1: ATPase H+ transporting V0 subunit e1; ATP6V1C2: ATPase H+ transporting V1 subunit C2; ATP6V1F: ATPase H+ transporting V1 subunit F; CAC: colitis-associated colorectal cancer; CRC: colorectal cancer; CTSB: cathepsin B; CTSG: cathepsin G; DEGs: differentially expressed genes; DSS: dextran sulfate sodium; FOXA2: forkhead box protein A2; F2RL1: F2R like trypsin receptor 1; IBD: inflammatory bowel disease; IECs: intestinal epithelial cells; LAMP1: lysosomal associated membrane protein 1; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; ROS: reactive oxygen species; SQSTM1/p62: sequestosome 1; TFs: transcription factors; UC: ulcerative colitis.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2130-2147"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459351/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144000435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction.","authors":"","doi":"10.1080/15548627.2025.2450891","DOIUrl":"10.1080/15548627.2025.2450891","url":null,"abstract":"","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"xv"},"PeriodicalIF":14.3,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12459369/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143495023","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inflammatory signaling attenuates spliceosome function and cognitive ability.","authors":"Lan Lin, Xiaoya Huang, Chunhua Huang, Juan Zou, Mengxin Hu, Tian Lan, Haoyu Wang, Zhuoyue Du, Mingfu Tian, Jiejie Liu, Huimin Dong, Baohui Liu, Hanhua Cheng, Li Zhou, Yu Chen, Rongjia Zhou","doi":"10.1080/15548627.2025.2562882","DOIUrl":"10.1080/15548627.2025.2562882","url":null,"abstract":"<p><p>Cognitive impairment is a complex condition with diverse causes, but the underlying mechanisms remain elusive. In this study, to explore whether and how inflammation affects cognitive impairment, we adopted two inflammation mouse models, coronavirus disease 2019 (COVID-19) inflammation and acute kidney injury (AKI)-induced inflammation. We observed that the inflammatory response caused accumulation of the oligomer marker derived from the short form of cleaved APP in the brain and cognitive impairment, which was associated with inflammation-induced activation of FGF2 in the mice. Notably, upon FGF2 activation, the HNRNPA1 was partially translocated from the nucleus to the cytoplasm and was degraded by macroautophagy/autophagy. Concurrently, a decrease in the nuclear HNRNPA1 levels impaired autophagy ability through downregulating ATG16L1α isoform via skipped exons in the brain of inflammation mice, thus attenuating autophagic clearance of the oligomers in the brain. The accumulation of the oligomers in the hippocampus region and cognitive impairment were also detected in FGF2-treated mice, owing to autophagy downregulation. Moreover, inhibiting FGF2 signaling via erdafitinib, an inhibitor of FGFR (fibroblast growth factor receptor) protein, partially restored autophagy and cognitive ability. Notably, autophagy ability was upregulated and the corresponding cognitive impairment were rescued in the <i>fgf2</i> knockout mice, under AKI conditions, due to retention of HNRNPA1 in the nucleus, and inhibition of the aberrant splicing of <i>ATG16L1</i>. These observations suggest that inflammation activates FGF2 signaling and attenuates autophagy, thus precipitating cognitive impairment.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-19"},"PeriodicalIF":14.3,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145082687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Urolithin Α modulates inter-organellar communication via calcium-dependent mitophagy to promote healthy ageing.","authors":"Antonis Roussos, Katerina Kitopoulou, Fivos Borbolis, Christina Ploumi, Despoina D Gianniou, Zhiquan Li, Haijun He, Eleni Tsakiri, Helena Borland, Ioannis K Kostakis, Martina Samiotaki, Ioannis P Trougakos, Vilhelm A Bohr, Konstantinos Palikaras","doi":"10.1080/15548627.2025.2561073","DOIUrl":"10.1080/15548627.2025.2561073","url":null,"abstract":"&lt;p&gt;&lt;p&gt;Mitochondrial dysfunction and impaired mitophagy are hallmarks of ageing and age-related pathologies. Disrupted inter-organellar communication among mitochondria, endoplasmic reticulum (ER), and lysosomes, further contributes to cellular dysfunction. While mitophagy has emerged as a promising target for neuroprotection and geroprotection, its potential to restore age-associated defects in organellar crosstalk remains unclear. Here, we show that mitophagy deficiency deregulates the morphology and homeostasis of mitochondria, ER and lysosomes, mirroring age-related alterations. In contrast, Urolithin A (UA), a gut-derived metabolite and potent mitophagy inducer, restores inter-organellar communication via calcium signaling, thereby, promoting mitophagy, healthspan and longevity. Our multi-omic analysis reveals that UA reorganizes ER, mitochondrial and lysosomal networks, linking inter-organellar dynamics to mitochondrial quality control. In &lt;i&gt;Caenorhabditis elegans&lt;/i&gt;, UA induces calcium release from the ER, enhances lysosomal activity, and drives DRP-1/DNM1L/DRP1-mediated mitochondrial fission, culminating in efficient mitophagy. Calcium chelation abolishes UA-induced mitophagy, blocking its beneficial impact on muscle function and lifespan, underscoring the critical role of calcium signaling in UA's geroprotective effects. Furthermore, UA-induced calcium elevation activates mitochondrial biogenesis via UNC-43/CAMK2D and SKN-1/NFE2L2/Nrf2 pathways, which are both essential for healthspan and lifespan extension. Similarly, in mammalian cells, UA increases intracellular calcium, enhances mitophagy and mitochondrial metabolism, and mitigates stress-induced senescence in a calcium-dependent manner. Our findings uncover a conserved mechanism by which UA-induced mitophagy restores inter-organellar communication, supporting cellular homeostasis and organismal health.&lt;b&gt;Abbreviations&lt;/b&gt;: Ca&lt;sup&gt;2+&lt;/sup&gt;: calcium ions; BJ: human foreskin fibroblasts; BNIP3: BCL2 interacting protein 3; BP: bipyridyl; CAMK2D: calcium/calmodulin dependent protein kinase II delta; CCCP: carbonyl cyanide m-chlorophenyl hydrazone; DEGs: differentially expressed genes; DEPs : differentially expressed peptides; DFP: deferiprone; DNM1L/DRP1: dynamin 1 like; EGTA: ethylene glycol bis(2-aminoethyl ether)-N,N,N',N'-tetraacetic acid; EMC: endoplasmic reticulum membrane protein complex; ER: endoplasmic reticulum; FCCP: carbonyl cyanide p-trifluoro-methoxyphenyl hydrazone; GO: gene ontology; GSVA: Gene Set Variation Analysis; HUVECs: human umbilical vein endothelial cells; IMM: inner mitochondrial membrane; ITPR/InsP3R: inositol 1,4,5-triphosphate receptor; MAM: mitochondria-associated ER membrane; MAPK: mitogen-activated protein kinase; MCU: mitochondrial calcium uniporter; MEFs: mouse embryonic fibroblasts; NAC : N-acetylcysteine; NFE2L2/Nrf2: NFE2 like bZIP transcription factor 2; NMN: nicotinamide mononucleotide; NR: nicotinamide riboside; OMM: outer mitochondrial membrane; ","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-26"},"PeriodicalIF":14.3,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145056179","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Non-canonical role of ATG4B in PRMT1-mediated DNA repair and leukemia progression.","authors":"Zhenkun Wang, Yuting Fu, Shuyi Lin, Yuanyuan Zhou, Qiongdan Gao, YanHong Xiao, Zhenyu Ju, Bo Liu","doi":"10.1080/15548627.2025.2564225","DOIUrl":"10.1080/15548627.2025.2564225","url":null,"abstract":"<p><p>Accumulating evidence indicates that many ATG (autophagy related) proteins perform non-canonical functions beyond their canonical roles in autophagy, particularly when they localize to subcellular compartments outside the cytoplasm. Although the autophagic functions of ATG4B (autophagy related 4B, cysteine peptidase) are well established, its potential non-canonical roles, especially under metabolic stress, remain largely unexplored. In our recent study, we show that energy deprivation induces autophagy-independent nuclear translocation of ATG4B. In the nucleus, ATG4B interacts with and cleaves PRMT1 (protein arginine methyltransferase 1), thereby reducing PRMT1-mediated methylation of the DNA-repair nuclease MRE11 and consequently impairing DNA repair. Notably, ATG4B is significantly upregulated in acute myeloid leukemia (AML) and shows prominent nuclear accumulation. Genetic knockdown or pharmacological inhibition of ATG4B in AML cells restores DNA repair capacity, activates the cell-cycle checkpoint kinase CHEK1/CHK1, attenuates malignant progression, and ultimately delays leukemia progression. These findings reveal an autophagy-independent role for nuclear ATG4B that links metabolic stress to the suppression of DNA repair and identify ATG4B as a potential therapeutic target in AML.<b>Abbreviation:</b> ATG, autophagy related; ATG4B, autophagy related 4B, cysteine peptidase; AML, acute myeloid leukemia; MAP1LC3/LC3, microtubule-associated protein 1 light chain 3; NES, nuclear export signal; NLS, nuclear localization signal; PE, phosphatidylethanolamine; PRMT1, protein arginine methyltransferase 1; UVRAG, UV radiation resistance associated gene.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145088197","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}