Autophagy最新文献

{"title":"TFEB and TFE3 regulate STING1-dependent immune responses by controlling type I interferon signaling.","authors":"Pablo J Tapia, José A Martina, Pablo S Contreras, Akriti Prashar, Eutteum Jeong, Dominic De Nardo, Rosa Puertollano","doi":"10.1080/15548627.2025.2487036","DOIUrl":"10.1080/15548627.2025.2487036","url":null,"abstract":"<p><p>STING1 is an essential component of the innate immune defense against a wide variety of pathogens. Whereas induction of type I interferon (IFN) responses is one of the best-defined functions of STING1, our transcriptomic analysis revealed IFN-independent activities of STING1 in macrophages, including transcriptional upregulation of numerous lysosomal and autophagic genes. This upregulation was mediated by the STING1-induced activation of the transcription factors TFEB and TFE3, and led to increased autophagy, lysosomal biogenesis, and lysosomal acidification. TFEB and TFE3 also modulated IFN-dependent STING1 signaling by controlling IRF3 activation. IFN production and cell death were increased in TFEB- and TFE3-depleted iBMDMs. Conversely, TFEB overexpression led to reduced IRF3 activation and an almost complete inhibition of IFN synthesis and secretion, resulting in decreased CASP3 activation and increased cell survival. Our study reveals a key role of TFEB and TFE3 as regulators of STING1-mediated innate antiviral immunity.<b>Abbreviation:</b> ACOD1/IRG1, aconitate decarboxylase 1; cGAMP, cyclic guanosine monophosphate-adenosine monophosphate; CGAS, cyclic GMP-AMP synthase; DMXAA, 5,6-dimethylxanthenone-4-acetic acid; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; GABARAP, GABA type A receptor-associated protein; HSV-1, herpes simplex virus type; iBMDMs, immortalized bone marrow-derived macrophages; IFN, type I interferon; IFNB, interferon beta; IKBKE, inhibitor of nuclear factor kappa B kinase subunit epsilon; IRF3, interferon regulatory factor 3; LAMP1, lysosomal associated membrane protein 1; LAMP2, lysosomal associated membrane protein 2; MTORC1, mechanistic target of rapamycin kinase complex 1; RPS6, ribosomal protein S6; STING1, stimulator of interferon response cGAMP interactor 1; TBK1, TANK binding kinase 1; TFE3, transcription factor binding to IGHM enhancer 3; TFEB, transcription factor EB.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2028-2045"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12363505/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143805130","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":"Pathological aging is alleviated by neutralization of the autophagy-repressive tissue hormone DBI/ACBP.","authors":"Léa Montégut, Flavia Lambertucci, Lucas Moledo-Nodar, Isabelle Martins, Alejandro Lucia, Clea Barcena, Guido Kroemer","doi":"10.1080/15548627.2025.2549451","DOIUrl":"10.1080/15548627.2025.2549451","url":null,"abstract":"<p><p>DBI/ACBP (diazepam binding inhibitor, acyl CoA-binding protein) is a macroautophagy/autophagy-inhibitory tissue hormone produced by multiple cell types. The plasma levels of DBI/ACBP rise with age and disease. In centenarians living in nursing homes, DBI/ACBP concentrations are approximately threefold higher than in younger adults (30-48 years old), but these levels increase further in centenarians hospitalized due to disease exacerbation. Elevated DBI/ACBP correlates with unfavorable clinical parameters, including high Charlson Comorbidity Index, elevated neutrophil:lymphocyte ratio, and decreased renal function. In mouse models, neutralization of DBI/ACBP using monoclonal antibodies ameliorates several aging-related pathologies. In <i>zmpste24</i>^<i>-/-</i> progeroid mice, anti-DBI/ACBP therapy improves posture, mobility, cutaneous and dental abnormalities, splenic atrophy, kidney function, and blood parameters. In models of renal aging induced by cisplatin or doxorubicin, DBI/ACBP neutralization suppresses renal fibrosis and cellular senescence. Similarly, in cardiac and hepatic aging models, anti-DBI/ACBP reduces expression of the senescence marker CDKN1A/p21 (cyclin dependent kinase inhibitor 1A) in cardiomyocytes and hepatocytes. Single-nucleus RNA sequencing of heart tissue revealed that anti-DBI/ACBP restores key metabolic and cardioprotective gene expression patterns suppressed by doxorubicin. Together, these findings establish DBI/ACBP as a marker and driver of pathological aging and demonstrate that its neutralization confers multi-organ anti-senescence effects. Thus, DBI/ACBP-targeting strategies hold therapeutic potential for improving healthspan.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144884447","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":"Corrigendum.","authors":"","doi":"10.1080/15548627.2025.2508380","DOIUrl":"10.1080/15548627.2025.2508380","url":null,"abstract":"","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"i"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12363498/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144210471","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":"Unconventional role of ATG16L1 in the control of ATP compartmentalization during apoptosis.","authors":"Elena Terraza-Silvestre, Julia Bandera-Linero, Daniel Oña-Sánchez, Felipe X Pimentel-Muiños","doi":"10.1080/15548627.2025.2519051","DOIUrl":"10.1080/15548627.2025.2519051","url":null,"abstract":"<p><p>The autophagy mediator ATG16L1 forms part of a complex that is essential for MAP1LC3/LC3 lipidation and autophagosome formation in the canonical macroautophagic/autophagic pathway. However, ATG16L1 is also involved in unconventional activities where LC3 becomes lipidated in single-membrane structures unrelated to double-membrane autophagosomes. Such atypical activities usually require the C-terminal domain of the molecule that includes 7 WD40-type repetitions (WD40 domain, WDD). The WDD acts as a docking site for upstream inducers that engage the LC3 lipidation ability of ATG16L1 in alternative membrane compartments. Given that this domain is absent in the yeast Atg16 ortholog, an intriguing idea proposes that it was added to the primitive protein during evolution to perform new physiological roles required by the appearance of multicellularity. Identification of such atypical activities and their physiological implications at the organismal level are important issues that remain to be clarified. In a recent report we describe an unconventional autophagic pathway that restrains the immunogenic potential of apoptosis, a key feature of homeostatic and developmentally regulated cell death in multicellular organisms. This signaling route emanates from apoptotic mitochondria and induces the formation of single-membrane, LC3-positive vesicles through a mechanism that requires the WDD of ATG16L1. The induced vesicles sequester ATP to inhibit the amount of ATP released from apoptotic cells and, consequently, prevent the activation of co-cultured phagocytes. Thus, this is a pathway that contributes to maintain the immunosilent nature of apoptotic cell death.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2085-2087"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12363522/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144287524","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":"PRMT1 (protein arginine methyltransferase 1) is essential for neuromuscular junction and mitochondrial homeostasis via mitophagy regulation.","authors":"Ju-Hyeon Bae, Chang-Lim You, Yideul Jeong, June Kim, Jinwoo Lee, Hyeon-Ju Jeong, Hyebeen Kim, Tuan Anh Vuong, Youngdae Gwon, Gyu-Un Bae, Jong-Sun Kang","doi":"10.1080/15548627.2025.2551477","DOIUrl":"https://doi.org/10.1080/15548627.2025.2551477","url":null,"abstract":"<p><p>The neuromuscular junction (NMJ) is essential for transmitting neural stimulus to muscles, triggering muscle contraction. Mitochondria are enriched in NMJ to support the energy needs required for neuromuscular function and stability. Thus, maintaining mitochondrial homeostasis through the clearance of damaged mitochondria, a process known as mitophagy, is vital for preserving neuromuscular health. Here, we highlight the crucial role of muscle PRMT1 in maintaining NMJ and mitochondrial homeostasis via mitophagy regulation. PRMT1 is distinctively expressed in myofibers, accumulating in the postsynaptic area, with its levels upregulated in denervated muscles. PRMT1-ablated muscles displayed disrupted NMJs and an accumulation of abnormal mitochondria, accompanied by increased mitochondrial oxidative stress. Additionally, <i>prmt1</i> depletion in muscles specifically impaired TBK1 (TANK binding kinase 1)-OPTN (optineurin)-mediated mitophagy. Overall, our findings suggest that PRMT1 plays a critical role in maintaining NMJ and mitochondrial health by regulating selective mitophagy through TBK1-OPTN.<b>Abbreviations:</b> ADMA: asymmetric arginine dimethylation; BTX: α-bungarotoxin; EDL: extensor digitorum longus; FDB: flexor digitorum brevis; GAS: gastrocnemius; NMJ: Neuromuscular junction; Mko: mice with muscle-specific <i>prmt1</i> ablation; MTOR: mechanistic target of rapamycin kinase; OPTN: optineurin; PRMT1: protein arginine methyltransferase 1; SA: sodium arsenate; SNI: sciatic nerve crush injury; Sol: soleus; SQSTM1/p62: sequestosome 1; TBK1: TANK binding kinase 1; TOMM20: translocase of outer mitochondrial membrane 20; TA: tibialis anterior; VDAC1: voltage dependent anion channel 1.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-18"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144982248","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":"EPG-5 regulates TGFB/TGF-β and WNT signalling by modulating retrograde endocytic trafficking.","authors":"Chongzhen Yuan, Huachuan Dong, Chunyan Wu, Jinyang Liu, Zheng Wang, Xingwei Wang, Haiyan Ren, Zhaoyu Wang, Qun Lu","doi":"10.1080/15548627.2025.2485420","DOIUrl":"10.1080/15548627.2025.2485420","url":null,"abstract":"<p><p>The Vici syndrome protein EPG5 acts as a tethering factor determining the fusion specificity of autophagosomes with late endosomes/lysosomes. Here we demonstrated that during <i>C. elegans</i> development, EPG-5 modulates SMA and MAB TGFB/TGF-β signaling in controlling body size and also WNT signaling in regulating cell migration. EPG-5 is required for retrograde trafficking of the TGFB receptor SMA-6 and WLS/Wntless homolog MIG-14. In <i>epg-5</i> mutants, SMA-6 and MIG-14 are trapped within hybrid endosomal structures, which colocalize with SNX-1- and SNX-3-labeled vesicles, respectively. Basolateral recycling processes of transmembrane cargos H.s.TFR/hTfR and H.s.IL2RA/hTAC are also defective in <i>epg-5</i> mutants. Depletion of EPG-5 causes defective RAB-5 and RAB-7, and RAB-5 and RAB-10 conversion, leading to the formation of these hybrid vesicles. The defects in endocytic trafficking and autophagy in <i>epg-5</i> mutants are ameliorated by knocking down components of the HOPS complex. Our study demonstrates the intersection between the autophagy pathway and the endocytic pathway, providing insights into the pathogenesis of amyotrophic lateral sclerosis (ALS) and Vici syndrome.<b>Abbreviations:</b> ALM: anterior lateral microtubule; ATG: autophagy related; AVM: anterior ventral microtubule; CORVET: class C core vacuole/endosome tethering; DAF-4: abnormal dauer formation 4; DIC: differential interference contrast; EPG: ectopic PGL granules; EPG-5: ectopic P granules 5; GAP: GTPase activating protein; GFP: green fluorescent protein; HOPS: homotypic fusion and vacuole protein sorting; H.s.IL2RA/hTAC: human interleukin 2 receptor subunit alpha; H.s.TFR/hTfR: human transferrin receptor; L1/L4: the first/fourth larval; mCh: mCherry; MIG-14: abnormal cell migration 14; PLM: posterior lateral microtubule; PVM: posterior ventral microtubule; RAB: ras-related protein; RFP: red fluorescent protein; RME-1: receptor mediated endocytosis 1; SMA-6: small 6; SNARE: soluble N-ethylmaleimide-sensitive factor attachment protein receptor; SNX: sorting nexin; TBC-2: TBC1 (Tre-2/Bub2/Cdc16) domain family 2; TGFB/TGF-β: transforming growth factor beta; TGN: trans-Golgi network; VPS: related to yeast vacuolar protein sorting factor; WT: wild type.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1995-2008"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12363523/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143733602","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":"Overlapping functions between <i>Lamp2a</i> and <i>Lamp2b</i> in cardiac autophagy.","authors":"Marina Sampaio Cruz, Ana Maria Manso, Angel Soto-Hermida, Paul Bushway, Elizabeth Silver, Betul Beyza Gunes, Zhiyuan Tang, Giovanni Gonzalez, Sharon Lau, Jordan Arbayo, Rita H Najor, Liguo Chi, Yusu Gu, Wei Feng, Randy T Cowling, Asa B Gustafsson, Ju Chen, Eric D Adler","doi":"10.1080/15548627.2025.2484620","DOIUrl":"10.1080/15548627.2025.2484620","url":null,"abstract":"<p><p>LAMP2 is a ubiquitously expressed protein critical for autophagy. Alternative splicing gives rise to three isoforms. However, the roles of major LAMP2 isoforms in the heart are not known. To address this knowledge gap, we generated <i>lamp2a</i> and <i>lamp2b</i> knockout (KO) mice to investigate the role of these isoforms in heart function and autophagy. Deletion of either <i>Lamp2a</i> or <i>Lamp2b</i> did not alter cardiac structure or function. Lack of all LAMP2 isoforms led to increased cardiac fibrosis and reduced survival during pressure overload, which were not observed in <i>lamp2a</i> or <i>lamp2b</i> KO mice. Also, LAMP2B loss did not affect levels of the autophagy markers LC3-II and SQSTM1/p62. Conversely, LAMP2A was upregulated in hearts lacking LAMP2B, potentially preserving autophagy and cardiac function. Reintroducing LAMP2A in <i>lamp2</i> KO mice effectively reduced autophagosome accumulation and improved cardiac function. Overall, these data support LAMP2 isoform functional redundancy in the myocardium under pathological conditions.<b>Abbreviations</b>: AAV: adeno-associated virus; ACTA2: actin alpha 2, smooth muscle, aorta; CMA: chaperone-mediated autophagy; KO: knockout; LAMP2: lysosomal-associated membrane protein 2; LV: Left ventricle; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; NPPA: natriuretic peptide type A; NPPB: natriuretic peptide type B; SQSTM1/p62: sequestosome 1; PBS: phosphate-buffered saline; PCR: polymerase chain reaction; TAC: transverse aortic constriction; WT: wild type.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"2046-2057"},"PeriodicalIF":14.3,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12366817/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143813214","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":"N-degron-mediated ATG8 isoform switching controls plant thermotolerance.","authors":"Seu Ha Kim, Ohkmae K Park","doi":"10.1080/15548627.2025.2552904","DOIUrl":"https://doi.org/10.1080/15548627.2025.2552904","url":null,"abstract":"<p><p>Macroautophagy/autophagy is a highly conserved catabolic pathway in eukaryotes that mediates the selective degradation and recycling of cellular components through the formation of double-membrane autophagosomes. ATG8 is a core component of autophagy and determines cargo selectivity through interactions with specific cargo receptors. Higher plants harbor multiple ATG8 isoforms, implying potential functional diversification; however, the biological significance of this isoform expansion remains largely unexplored. In a recent study, we identified UBR7 (UBIQUITIN PROTEIN LIGASE E3 COMPONENT N-RECOGNIN 7) as a novel N-recognin that targets ATG8a for proteasomal degradation via the Arg/N-degron pathway. This selective degradation triggers isoform switching by enabling the replacement of ATG8a with alternative ATG8 isoforms. Notably, this process occurs specifically during the recovery phase following heat stress and plays a critical role in enhancing thermotolerance. Our findings provide new insights into the functional specialization and dynamic regulation of ATG8 isoforms in plants and suggest new directions for improving crop resilience under climate-associated temperature fluctuations.<b>Abberivations</b> HS, heat stress: HSP, heat shock protein; RBP, RNA-binding protein; UTR, untranslated region.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2025-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144982274","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":"<i>Salmonella</i> Typhimurium exploits the reticulophagy/ERphagy receptor RETREG1 to promote infection.","authors":"Damian Gatica, Reham Alsaadi, Ryan C Russell","doi":"10.1080/15548627.2025.2551672","DOIUrl":"https://doi.org/10.1080/15548627.2025.2551672","url":null,"abstract":"<p><p>Macroautophagy/autophagy is a key catabolic-recycling pathway that can selectively target damaged organelles or invading pathogens for degradation. The selective autophagic degradation of the endoplasmic reticulum, called reticulophagy/ERphagy, controls ER size and degradation of misfolded protein aggregates. RETREG1/FAM134B is an ERphagy receptor that acts by inducing ER membrane curvature and scission through oligomerization. Interestingly, RETREG1 has also been implicated in the cellular response against pathogen infection. Multiple microbes have developed strategies to inhibit ERphagy by targeting RETREG1. In a recent study, we characterized an unidentified mechanism of bacterial-mediated inhibition of ERphagy. Specifically, we found that <i>Salmonella enterica</i> Serovar Typhimurium, a well-known intracellular pathogen that continues to be a major cause of foodborne infections worldwide, inhibits ERphagy by specifically targeting the activity of RETREG1, leading to a pronounced increase in <i>Salmonella</i> burden. We show that <i>Salmonella</i> prevents RETREG1 oligomerization, which is required for efficient ERphagy. Conversely, <i>Salmonella</i>-mediated ERphagy blockage can be bypassed by promoting RETREG1 oligomerization, which recovers ERphagy levels. <i>Salmonella</i> infection also decreases RETREG1 phosphorylation and acetylation, previously reported to be requisite steps in RETREG1-driven ERphagy. Furthermore, in vivo analysis of <i>retreg1</i> knockout mice infected with <i>Salmonella</i> reveals increased intestinal damage and bacterial levels. Our results provide insights into the interplay between ERphagy and bacterial infection, highlighting a key role for RETREG1 in innate immunity.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":"1-3"},"PeriodicalIF":14.3,"publicationDate":"2025-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144982284","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-coding RNAs regulate autophagy in kidney disease: friend or foe?","authors":"Yankun Li, Tongtong Ma, Xinhua Liang, Tingting Jin, Xingqi Zhao, Junmin Huang, Junfeng Hao, Huafeng Liu, Peng Wang","doi":"10.1080/15548627.2025.2551683","DOIUrl":"10.1080/15548627.2025.2551683","url":null,"abstract":"<p><p>Macroautophagy/autophagy is a conserved cellular process that degrades misfolded proteins and damaged organelles to regulate cell survival and division. Normal levels of autophagy are observed in healthy kidney cells. In contrast, excessive or insufficient autophagy is observed during kidney disease progression. However, canonical treatments that regulate autophagy using chemical reagents may induce unexpected side effects in other organs. This necessitates the development of therapeutic approaches with fewer adverse effects. Non-coding RNAs, which are highly tissue-specific, regulate autophagy and accurately modulate the expression of related genes. This review presents evidence of the effects of non-coding RNAs on the progression of kidney diseases and their responses to treatment <i>in vitro</i>, <i>in vivo</i>, and in clinical trials. Our analyses and interpretations of key findings elucidate the pathogenesis of kidney diseases and explore potential new therapeutic approaches.</p>","PeriodicalId":93893,"journal":{"name":"Autophagy","volume":" ","pages":""},"PeriodicalIF":14.3,"publicationDate":"2025-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144982306","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}