Autophagy reports最新文献_第2页

The nonsense-mediated mRNA decay factor Upf3 negatively regulates bulk autophagy progression in Saccharomyces cerevisiae. 无义介导的mRNA衰变因子Upf3负调控酿酒酵母的自噬进程。

Autophagy reports Pub Date : 2026-02-06 eCollection Date: 2026-01-01 DOI: 10.1080/27694127.2026.2623730

Tabassum Ahmad Tasmi, Emily Solomon, Emmanuella Wesome Avogo, Swaroopa Badenahalli Narasimhaiah, Elizabeth Delorme-Axford

{"title":"The nonsense-mediated mRNA decay factor Upf3 negatively regulates bulk autophagy progression in Saccharomyces cerevisiae.","authors":"Tabassum Ahmad Tasmi, Emily Solomon, Emmanuella Wesome Avogo, Swaroopa Badenahalli Narasimhaiah, Elizabeth Delorme-Axford","doi":"10.1080/27694127.2026.2623730","DOIUrl":"10.1080/27694127.2026.2623730","url":null,"abstract":"Macroautophagy/Autophagy is a highly conserved mechanism that targets cytoplasmic cargo for degradation and recycling. At present, 45 autophagy-related (ATG) genes have been identified in fungi. Due to this complexity, the autophagy pathway must be strictly regulated at multiple levels (transcriptional, post-transcriptional, translational, and post-translational). Dysregulation of autophagy can have detrimental effects on cell health and survival. Therefore, investigation into the mechanisms regulating autophagy is critical. The nonsense-mediated mRNA decay (NMD) pathway targets transcripts with premature translation termination codons (PTCs), although NMD also regulates normal transcripts. NMD requires conserved factors in yeast - Upf1, Upf2, and Upf3. Here, we demonstrate that autophagy activity increases in upf1∆ upf2∆ upf3∆ cells. We also show that autophagy is enhanced in upf3∆ cells through multiple assays. UPF3/Upf3 expression decreases during starvation and autophagy induction. Loss of UPF3 results in the upregulation of ATG16/Atg16, which is required for autophagosome formation. Furthermore, ATG16 is likely targeted by NMD. These findings provide insight into how yeast cells may modulate autophagy through the mRNA decay factor Upf3.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"5 1","pages":"2623730"},"PeriodicalIF":0.0,"publicationDate":"2026-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12885402/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146159508","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}

引用次数: 0

ATG9A-dependent, LC3-independent autophagy curbs the immune system to protect against disease. atg9a依赖性、lc3非依赖性的自噬抑制免疫系统抵御疾病。

Autophagy reports Pub Date : 2026-01-12 eCollection Date: 2026-01-01 DOI: 10.1080/27694127.2026.2614147

Dario Priem, Mathieu Jm Bertrand

引用次数: 0

Glycophagy: molecular mechanisms, regulatory signals, and disease associations. 糖吞噬：分子机制、调节信号和疾病关联。

Autophagy reports Pub Date : 2026-01-08 eCollection Date: 2026-01-01 DOI: 10.1080/27694127.2025.2595375

Lei Chen, Jinyong Jiang, Meiqing Liu, Linxi Chen

{"title":"Glycophagy: molecular mechanisms, regulatory signals, and disease associations.","authors":"Lei Chen, Jinyong Jiang, Meiqing Liu, Linxi Chen","doi":"10.1080/27694127.2025.2595375","DOIUrl":"10.1080/27694127.2025.2595375","url":null,"abstract":"Glycophagy is a process of selective degradation of glycogen through the autophagy pathway. It relies on key proteins, such as STBD1 (glycogen-specific autophagy receptor), GABARAPL1 (member of the ATG8 family), and acid α-glucosidase (GAA), and proceeds through the steps of \"glycogen recognition - autophagosome encapsulation - lysosomal degradation\" to release glucose, thereby maintaining energy homeostasis. This process is regulated by multiple signaling pathways, such as AMPK, mTOR, CAMP/PKA, and calcium signaling pathways, which jointly respond to cellular energy demands and metabolic states. Glycophagy occurs under conditions, such as starvation, exercise, and energy metabolism disorders, and plays a role in diseases with glycogen metabolism disorders. Its functions include energy supply, blood sugar regulation, maintenance of cellular homeostasis, and influencing cellular aging. Dysfunction of glycophagy can lead to various diseases, such as glycogen storage diseases and diabetic cardiomyopathy. In-depth study of the regulatory mechanisms of glycophagy is helpful for developing therapeutic strategies for related diseases.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"5 1","pages":"2595375"},"PeriodicalIF":0.0,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12785236/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145954103","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}

引用次数: 0

RETREG1/FAM134B-mediated micro-ER-phagy in the retrovirus-SERINC5 arms race. 逆转录病毒- serinc5军备竞赛中RETREG1/ fam134b介导的微er吞噬

Autophagy reports Pub Date : 2025-12-19 eCollection Date: 2026-01-01 DOI: 10.1080/27694127.2025.2602971

Jim Maurice Camilleri, Iqbal Ahmad, Jing Zhang, Sunan Li, Yong-Hui Zheng

{"title":"RETREG1/FAM134B-mediated micro-ER-phagy in the retrovirus-SERINC5 arms race.","authors":"Jim Maurice Camilleri, Iqbal Ahmad, Jing Zhang, Sunan Li, Yong-Hui Zheng","doi":"10.1080/27694127.2025.2602971","DOIUrl":"10.1080/27694127.2025.2602971","url":null,"abstract":"Reticulophagy regulator 1 (RETREG1)/Family with sequence similarity 134 member B (FAM134B) is a selective endoplasmic reticulum (ER)-phagy receptor that mediates starvation-induced macro-ER-phagy, but whether it participates in other pathways mediating ER turnover has remained unclear. Here, we unveil a previously unrecognized role for RETREG1 in micro-ER-phagy and show how the murine leukemia virus (MLV) accessory protein glycosylated group-specific antigen (glycoGag) exploits this pathway to antagonize the host restriction factor SERINC5 (serine incorporator 5). GlycoGag binds SERINC5 in the endoplasmic reticulum (ER) and selectively recruits RETREG1 to eliminate SERINC5 through an autophagosome-independent process that bypasses ATG3 (autophagy-related), ATG5, ATG7, BECN1 (Beclin-1), LC3 (microtubule-associated protein 1 light chain 3) lipidation, and PIK3C3 (phosphatidylinositol 3-kinase catalytic subunit type 3)/hVPS34 (vacuolar protein sorting 34). RETREG1 knockout abolishes degradation of ER-retained SERINC5, whereas endolysosomal turnover of surface SERINC5 remains partially intact, demonstrating that glycoGag utilizes dual ER-phagy and endolysosomal routes to suppress SERINC5. These findings expand the functional repertoire of RETREG1 in autophagy, identify that retroviruses repurpose micro-ER-phagy to circumvent SERINC5-mediated restriction, and reveal ER-phagy as an understudied battleground in the ongoing arms race between cellular restriction factors and viral accessory proteins.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"5 1","pages":"2602971"},"PeriodicalIF":0.0,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12721084/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145822181","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}

引用次数: 0

TFEB-mediated autophagy stimulation as an anabolic strategy for bone: insights from TFEB activation in the osteoblast lineage. TFEB介导的自噬刺激作为骨的合成代谢策略：来自成骨细胞谱系中TFEB激活的见解。

Autophagy reports Pub Date : 2025-12-08 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2596422

Melda Onal

{"title":"TFEB-mediated autophagy stimulation as an anabolic strategy for bone: insights from TFEB activation in the osteoblast lineage.","authors":"Melda Onal","doi":"10.1080/27694127.2025.2596422","DOIUrl":"10.1080/27694127.2025.2596422","url":null,"abstract":"Autophagy in the osteoblast lineage is essential for bone formation and skeletal homeostasis, yet the mechanisms through which it supports bone formation remain unclear. To investigate these mechanisms and evaluate the anabolic potential of autophagy stimulation, we generated a genetic mouse model in which transcription factor EB (Tfeb), a master regulator of autophagy and lysosomal biogenesis, was elevated specifically in osteoblast-lineage cells. Tfeb elevation increased the expression of autophagy and lysosomal genes and enhanced autophagic flux in osteoblasts. Stimulation of autophagy increased bone formation in both cortical and cancellous bone compartments, leading to gains in bone mass and strength. Single-cell RNA sequencing revealed reduced osteoblast apoptosis, suggesting improved cell survival as a contributor to the observed increase in osteoblast number. Our ex vivo studies also suggest that autophagy stimulation increases proliferation of osteoblats lineage cells. In addition to increasing osteoblast number, Tfeb elevation also enhanced osteoblast function, likely by increasing transcription and translation of extracellular bone matrix components. Taken together, these findings demonstrate that elevation of Tfeb in the osteoblast lineage cells stimulates autophagy, promotes bone formation, and leads to increased bone mass and strength, supporting further investigation of TFEB or autophagy activation as a potential therapeutic strategy for osteoporosis.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"4 1","pages":"2596422"},"PeriodicalIF":0.0,"publicationDate":"2025-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12688215/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145727488","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}

引用次数: 0

Involvement of ACSL3 in the formation of autophagosomes and lipid droplets during starvation conditions. 饥饿状态下ACSL3参与自噬体和脂滴的形成。

Autophagy reports Pub Date : 2025-12-02 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2593061

Shun Kato, Mitsuo Tagaya

{"title":"Involvement of ACSL3 in the formation of autophagosomes and lipid droplets during starvation conditions.","authors":"Shun Kato, Mitsuo Tagaya","doi":"10.1080/27694127.2025.2593061","DOIUrl":"10.1080/27694127.2025.2593061","url":null,"abstract":"Acyl-CoA synthetase long-chain (ACSL) catalyzes the conversion of fatty acids into acyl-CoA, which is used for neutral lipid and phospholipid synthesis. Previous studies revealed that yeast Faa1 and mammalian ACSL4 play a crucial role in phagophore expansion by locally synthesizing phospholipids. We found that another member of ACSL protein family, ACSL3, which is involved in lipid droplet biogenesis under energy-rich conditions and is regulated by SYNTAXIN17, also participates in autophagosome formation, but in a different manner. Knockdown of ACSL3 suppressed punctum formation of early autophagosomal marker proteins such as FIP200 and WIPI2 in starved cells, generating nonfunctional multi-membrane autophagosome-like structures. In contrast, ACSL4 suppression blocked autophagosome formation without affecting punctum formation of early autophagosomal marker proteins. Mechanistic analysis revealed that ACSL3 functions independently of its enzymatic activity, while catalytic activity of ACSL4 is required for autophagosome formation as well as LC3 (known as MAP1LC3 proteins) protein lipidation. Furthermore, ACSL3 has been shown to be essential for lipid droplet biogenesis during starvation. These findings establish ACSL3 as a key player in two events in early autophagy: formation of autophagosomes and lipid droplets.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"4 1","pages":"2593061"},"PeriodicalIF":0.0,"publicationDate":"2025-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12674330/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145679496","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}

引用次数: 0

Autophagy cargo profiles in skeletal muscle during starvation and exercise. 在饥饿和运动期间骨骼肌的自噬货物分布。

Autophagy reports Pub Date : 2025-12-02 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2593060

Mohd Farhan, Shangze Lyu, Trezze P Nguyen, Dakai Zhang, Hong Liang, Yong Zhou, Yu A An, Jun Wang, Hongyuan Yang, Guangwei Du, Yang Liu

{"title":"Autophagy cargo profiles in skeletal muscle during starvation and exercise.","authors":"Mohd Farhan, Shangze Lyu, Trezze P Nguyen, Dakai Zhang, Hong Liang, Yong Zhou, Yu A An, Jun Wang, Hongyuan Yang, Guangwei Du, Yang Liu","doi":"10.1080/27694127.2025.2593060","DOIUrl":"10.1080/27694127.2025.2593060","url":null,"abstract":"Autophagy is a cellular process to clear unwanted and dysfunctional cellular cargoes, which are sequestered in autophagosomes before their delivery to lysosomes for degradation. Autophagy cargo selection, mediated by cargo receptors, varies across cell types and conditions. Understanding the cargo features is essential for elucidating autophagy's function in specific physiological or pathological contexts. Here, we present a simple and rapid method for isolating LC3B-positive autophagosomes from the tissues of GFP-LC3 transgenic mice, a widely used autophagy reporter model, without relying on the complex ultracentrifugation steps required by traditional methods. When combined with quantitative proteomics, this approach enables efficient in vivo characterization of autophagy cargoes. We applied this method to establish autophagy cargo profiles in skeletal muscle during starvation and exercise, two physiological conditions that activate autophagy, and identified distinct cargo selection patterns, with significantly higher levels of ER-phagy and ribophagy observed during starvation. We further revealed the ER-phagy receptors TEX264 and RETREG1/FAM134B as potential mediators of the elevated ER-phagy under starvation. In summary, we report an efficient workflow for in vivo autophagy cargo characterization and provide detailed analysis and comparison of cargo profiles under starvation and exercise conditions.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"4 1","pages":"2593060"},"PeriodicalIF":0.0,"publicationDate":"2025-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12674447/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145679510","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}

引用次数: 0

Illuminating the regulatory link between blue light and autophagy in photomorphogenesis. 阐明光形态发生中蓝光与自噬之间的调控联系。

Autophagy reports Pub Date : 2025-11-14 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2586831

Lu Jiang, Hong-Quan Yang, Wenxiu Wang

引用次数: 0

Deacetylation of HSC70 by SIRT2 promotes chaperone mediated autophagy. SIRT2介导的HSC70去乙酰化促进伴侣蛋白介导的自噬。

Autophagy reports Pub Date : 2025-11-12 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2580781

Byunghyun Ahn, Wenzhe Chen, Wenbiao Shi, Ruben Shrestha, Fenghua Hu, Hening Lin

{"title":"Deacetylation of HSC70 by SIRT2 promotes chaperone mediated autophagy.","authors":"Byunghyun Ahn, Wenzhe Chen, Wenbiao Shi, Ruben Shrestha, Fenghua Hu, Hening Lin","doi":"10.1080/27694127.2025.2580781","DOIUrl":"10.1080/27694127.2025.2580781","url":null,"abstract":"Chaperone-mediated autophagy (CMA) is a selective form of lysosomal protein degradation essential for cellular proteostasis. CMA is activated during cellular stress, such as starvation, and involves the chaperone protein HSC70 (HSPA8) recognizing substrates containing KFERQ-like motifs. However, the regulatory mechanisms governing CMA activation remain poorly understood. Here, we demonstrate that the NAD+ -dependent deacetylase SIRT2 promotes CMA activation by deacetylating HSC70 at lysine 557 (K557). Our findings reveal that SIRT2 activity is upregulated during starvation, enhancing its interaction with HSC70 and facilitating the deacetylation of K557. Deacetylation of HSC70 at K557 increases its binding affinity to CMA substrates, thereby promoting their lysosomal degradation. Mutation of K557 to a deacetylation-mimetic arginine (K557R) enhances CMA activity under both nutrient-rich and starvation conditions, while the acetylation-mimetic glutamine mutant (K557Q) impairs substrate binding and CMA activation. Furthermore, the inhibition or knockdown of SIRT2 reduces CMA activity, which is rescued by HSC70 K557R expression. These findings identify SIRT2-mediated deacetylation of HSC70 as a regulatory mechanism for CMA activation during nutrient deprivation and highlight the role of protein lysine acetylation in proteostasis. This study provides insights into the interplay between SIRT2, HSC70, and CMA, with potential implications for diseases linked to proteostasis dysregulation, including neurodegenerative disorders and cancer.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"4 1","pages":"2580781"},"PeriodicalIF":0.0,"publicationDate":"2025-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12622308/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145552086","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}

引用次数: 0

CNX:FAM134B-driven ERLAD of ATZ polymers proceeds via enhanced formation of VAPA:ORP1L:RAB7 contact sites between ER and endolysosomes. CNX: fam134b驱动的ATZ聚合物的ERLAD通过增强内质网和内溶酶体之间的VAPA:ORP1L:RAB7接触位点的形成进行。

Autophagy reports Pub Date : 2025-10-30 eCollection Date: 2025-01-01 DOI: 10.1080/27694127.2025.2574355

Elisa Fasana, Ilaria Fregno, Maurizio Molinari

{"title":"CNX:FAM134B-driven ERLAD of ATZ polymers proceeds via enhanced formation of VAPA:ORP1L:RAB7 contact sites between ER and endolysosomes.","authors":"Elisa Fasana, Ilaria Fregno, Maurizio Molinari","doi":"10.1080/27694127.2025.2574355","DOIUrl":"10.1080/27694127.2025.2574355","url":null,"abstract":"Membrane contact sites (MCS) between organelles maintain the proximity required for controlled exchange of small molecules and ions yet preventing fusion events that would compromise organelles' identity and integrity. Here, by investigating the intracellular fate of the disease-causing Z-variant of alpha1 antitrypsin (ATZ), we report on a novel function of MCS between the endoplasmic reticulum (ER) and RAB7/LAMP1-positive endolysosomes in ER-to-lysosome-associated degradation (ERLAD). For this function, the VAPA:ORP1L:RAB7 multi-protein complex forming MCS between the ER and endolysosomes engages, in an ERLAD client-driven manner, the misfolded protein segregation complex formed by the lectin chaperone calnexin (CNX), the ER-phagy receptor FAM134B, and the ubiquitin-like protein LC3. Generation of this supramolecular complex facilitates the membrane fusion events regulated by the SNARE proteins STX17 and VAMP8 that ensure efficient delivery of ATZ polymers from their site of generation, the ER, to the site of their intracellular clearance, the degradative RAB7/LAMP1-positive endolysosomes.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"4 1","pages":"2574355"},"PeriodicalIF":0.0,"publicationDate":"2025-10-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12578312/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145433077","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}

引用次数: 0