Autophagy reportsPub Date : 2023-01-19DOI: 10.1080/27694127.2023.2166322
V. V. Kulkarni, Sandra Maday
{"title":"Sorting trash from treasure: Separate pathways for autophagy and endocytic trafficking in axons","authors":"V. V. Kulkarni, Sandra Maday","doi":"10.1080/27694127.2023.2166322","DOIUrl":"https://doi.org/10.1080/27694127.2023.2166322","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44457006","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}
Autophagy reportsPub Date : 2023-01-16DOI: 10.1080/27694127.2023.2166324
H. Kramer, Sarah A Allman
{"title":"Sugar coating autophagy: exploring the links between the inhibition of NGLY1 (N-glycanase 1) and autophagy induction","authors":"H. Kramer, Sarah A Allman","doi":"10.1080/27694127.2023.2166324","DOIUrl":"https://doi.org/10.1080/27694127.2023.2166324","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48364730","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}
Autophagy reportsPub Date : 2023-01-11DOI: 10.1080/27694127.2022.2163091
Sydney E. Cason, Saurabh S. Mogre, Elena F. Koslover, E. Holzbaur
{"title":"Neuronal Autophagy by the Numbers","authors":"Sydney E. Cason, Saurabh S. Mogre, Elena F. Koslover, E. Holzbaur","doi":"10.1080/27694127.2022.2163091","DOIUrl":"https://doi.org/10.1080/27694127.2022.2163091","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47769787","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}
Autophagy reportsPub Date : 2023-01-05DOI: 10.1080/27694127.2022.2164089
Anne Kristin McLaren Berge, Juncal Garcia-Garcia, E. Sjøttem, Hallvard Lauritz Olsvik
{"title":"The ubiquitin E3 ligase TRIM27 emerges as a new player in mitophagy","authors":"Anne Kristin McLaren Berge, Juncal Garcia-Garcia, E. Sjøttem, Hallvard Lauritz Olsvik","doi":"10.1080/27694127.2022.2164089","DOIUrl":"https://doi.org/10.1080/27694127.2022.2164089","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47284843","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}
Autophagy reportsPub Date : 2023-01-01DOI: 10.1080/27694127.2023.2166722
Ron Benyair, Sai Srinivas Panapakkam Giridharan, Pilar Rivero-Ríos, Junya Hasegawa, Emily Bristow, Eeva-Liisa Eskelinen, Merav D Shmueli, Vered Fishbain-Yoskovitz, Yifat Merbl, Lisa M Sharkey, Henry L Paulson, Phyllis I Hanson, Samarjit Patnaik, Ismael Al-Ramahi, Juan Botas, Juan Marugan, Lois S Weisman
{"title":"Upregulation of the ESCRT pathway and multivesicular bodies accelerates degradation of proteins associated with neurodegeneration.","authors":"Ron Benyair, Sai Srinivas Panapakkam Giridharan, Pilar Rivero-Ríos, Junya Hasegawa, Emily Bristow, Eeva-Liisa Eskelinen, Merav D Shmueli, Vered Fishbain-Yoskovitz, Yifat Merbl, Lisa M Sharkey, Henry L Paulson, Phyllis I Hanson, Samarjit Patnaik, Ismael Al-Ramahi, Juan Botas, Juan Marugan, Lois S Weisman","doi":"10.1080/27694127.2023.2166722","DOIUrl":"https://doi.org/10.1080/27694127.2023.2166722","url":null,"abstract":"<p><p>Many neurodegenerative diseases, including Huntington's disease (HD) and Alzheimer's disease (AD), occur due to an accumulation of aggregation-prone proteins, which results in neuronal death. Studies in animal and cell models show that reducing the levels of these proteins mitigates disease phenotypes. We previously reported a small molecule, NCT-504, which reduces cellular levels of mutant huntingtin (mHTT) in patient fibroblasts as well as mouse striatal and cortical neurons from an Hdh<sup>Q111</sup> mutant mouse. Here, we show that NCT-504 has a broader potential, and in addition reduces levels of Tau, a protein associated with Alzheimer's disease, as well as other tauopathies. We find that in untreated cells, Tau and mHTT are degraded via autophagy. Notably, treatment with NCT-504 diverts these proteins to multivesicular bodies (MVB) and the ESCRT pathway. Specifically, NCT-504 causes a proliferation of endolysosomal organelles including MVB, and an enhanced association of mHTT and Tau with endosomes and MVB. Importantly, depletion of proteins that act late in the ESCRT pathway blocked NCT-504 dependent degradation of Tau. Moreover, NCT-504-mediated degradation of Tau occurred in cells where Atg7 is depleted, which indicates that this pathway is independent of canonical autophagy. Together, these studies reveal that upregulation of traffic through an ESCRT-dependent MVB pathway may provide a therapeutic approach for neurodegenerative diseases.</p>","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10101321/pdf/nihms-1884781.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9328582","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}
Autophagy reportsPub Date : 2023-01-01Epub Date: 2023-05-17DOI: 10.1080/27694127.2023.2213541
Damián Lobato-Márquez, José Javier Conesa, Ana Teresa López-Jiménez, Michael E Divine, Jonathan N Pruneda, Serge Mostowy
{"title":"Interplay between septins and ubiquitin-mediated xenophagy during <i>Shigella</i> entrapment.","authors":"Damián Lobato-Márquez, José Javier Conesa, Ana Teresa López-Jiménez, Michael E Divine, Jonathan N Pruneda, Serge Mostowy","doi":"10.1080/27694127.2023.2213541","DOIUrl":"10.1080/27694127.2023.2213541","url":null,"abstract":"<p><p>Septins are cytoskeletal proteins implicated in numerous cellular processes including cytokinesis and morphogenesis. In the case of infection by <i>Shigella flexneri</i>, septins assemble into cage-like structures that entrap cytosolic bacteria targeted by autophagy. The interplay between septin cage entrapment and bacterial autophagy is poorly understood. We used a correlative light and cryo-soft X-ray tomography (cryo-SXT) pipeline to study septin cage entrapment of <i>Shigella</i> in its near-native state. Septin cages could be identified as X-ray dense structures, indicating they contain host cell proteins and lipids consistent with their autophagy links. Airyscan confocal microscopy of <i>Shigella</i>-septin cages showed that septins and lysine 63 (K63)-linked ubiquitin chains are present in separate bacterial microdomains, suggesting they are recruited separately. Finally, Cryo-SXT and live-cell imaging revealed an interaction between septins and microtubule-associated protein light chain 3B (LC3B)-positive membranes during autophagy of <i>Shigella</i>. Collectively our data present a new model for how septin-caged <i>Shigella</i> are targeted to autophagy.</p>","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10264059/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9671939","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}
Autophagy reportsPub Date : 2023-01-01Epub Date: 2023-03-01DOI: 10.1080/27694127.2023.2178996
Paloma B Liton, Kathleen Boesze-Battaglia, Michael E Boulton, Patricia Boya, Thomas A Ferguson, Ian G Ganley, Anu Kauppinnen, Gordon W Laurie, Noboru Mizushima, Hideaki Morishita, Rossella Russo, Jaya Sadda, Rajalekshmy Shyam, Debasish Sinha, Debra A Thompson, David N Zacks
{"title":"AUTOPHAGY IN THE EYE: FROM PHYSIOLOGY TO PATHOPHYSOLOGY.","authors":"Paloma B Liton, Kathleen Boesze-Battaglia, Michael E Boulton, Patricia Boya, Thomas A Ferguson, Ian G Ganley, Anu Kauppinnen, Gordon W Laurie, Noboru Mizushima, Hideaki Morishita, Rossella Russo, Jaya Sadda, Rajalekshmy Shyam, Debasish Sinha, Debra A Thompson, David N Zacks","doi":"10.1080/27694127.2023.2178996","DOIUrl":"10.1080/27694127.2023.2178996","url":null,"abstract":"<p><p>Autophagy is a catabolic self-degradative pathway that promotes the degradation and recycling of intracellular material through the lysosomal compartment. Although first believed to function in conditions of nutritional stress, autophagy is emerging as a critical cellular pathway, involved in a variety of physiological and pathophysiological processes. Autophagy dysregulation is associated with an increasing number of diseases, including ocular diseases. On one hand, mutations in autophagy-related genes have been linked to cataracts, glaucoma, and corneal dystrophy; on the other hand, alterations in autophagy and lysosomal pathways are a common finding in essentially all diseases of the eye. Moreover, LC3-associated phagocytosis, a form of non-canonical autophagy, is critical in promoting visual cycle function. This review collects the latest understanding of autophagy in the context of the eye. We will review and discuss the respective roles of autophagy in the physiology and/or pathophysiology of each of the ocular tissues, its diurnal/circadian variation, as well as its involvement in diseases of the eye.</p>","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10078619/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9708880","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}
Autophagy reportsPub Date : 2023-01-01Epub Date: 2023-08-01DOI: 10.1080/27694127.2023.2242054
Sheridan Mikhail, Scott A Soleimanpour
{"title":"Protein disorder in the regulatory control of mitophagy.","authors":"Sheridan Mikhail, Scott A Soleimanpour","doi":"10.1080/27694127.2023.2242054","DOIUrl":"10.1080/27694127.2023.2242054","url":null,"abstract":"<p><p>Mitophagy is a central component of the mitochondrial quality control machinery, which is necessary for cellular viability and bioenergetics. The E3 ubiquitin ligase CLEC16A (C-type lectin domain containing 16A) forms a tripartite mitophagy regulatory complex together with the E3 ligase RNF41 (ring finger protein 41) and the ubiquitin-specific peptidase USP8 (ubiquitin specific peptidase 8), yet CLEC16A structural/functional domains relevant for mitophagy are unknown. We identify that CLEC16A contains an internal intrinsically disordered region (IDR), which is important for CLEC16A function and stability. IDRs are flexible domains lacking fixed secondary structure and regulate an emerging number of diverse processes, yet they have been largely unstudied in mitophagy. We observe that the internal CLEC16A IDR is essential for CLEC16A degradation and is bound by RNF41 to promote CLEC16A turnover. This IDR also promotes assembly of the CLEC16A-RNF41-USP8 mitophagy regulatory complex. Thus, our study revealed the importance of IDRs in mitophagy via the regulation of CLEC16A abundance by RNF41, opening new structural insights into mitochondrial quality control.</p>","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"2 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10399515/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10316274","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}