Pub Date : 2023-11-22DOI: 10.1080/27694127.2023.2285214
Angela Dixon, M. Shim, April Nettesheim, Aislyn Coyne, Chien-Chia Su, Haiyan Gong, P. Liton
{"title":"Autophagy deficiency protects against ocular hypertension and glaucoma","authors":"Angela Dixon, M. Shim, April Nettesheim, Aislyn Coyne, Chien-Chia Su, Haiyan Gong, P. Liton","doi":"10.1080/27694127.2023.2285214","DOIUrl":"https://doi.org/10.1080/27694127.2023.2285214","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"20 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139247368","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}
Pub Date : 2023-11-14DOI: 10.1080/27694127.2023.2278946
O. Erlichman, Tamar Avin-Wittenberg
{"title":"Relative dependence: Autophagy in the mother plant and the embryo contributes to Arabidopsis seed development","authors":"O. Erlichman, Tamar Avin-Wittenberg","doi":"10.1080/27694127.2023.2278946","DOIUrl":"https://doi.org/10.1080/27694127.2023.2278946","url":null,"abstract":"","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"33 4","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139277162","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}
Pub Date : 2023-11-13DOI: 10.1080/27694127.2023.2277585
Pierre-Louis Tharaux, Olivia Lenoir
Pharmacological approaches aimed at increasing autophagic flux and genetically engineered mice with autophagy deficiency in the endothelium have demonstrated that autophagy exerts vessel protection against metabolic stresses and vascular aging. However, the identity of the specific cellular processes that autophagy controls in endothelial cells remained unclear. In this punctum, we discuss our recent findings on the multiple functions of autophagy in the endothelium. Particularly, we highlighted that autophagy controls flow-mediated vascular reactivity and remodeling. We have also focused on the role of autophagy machinery in regulating protein distribution within the cell and on the results demonstrating how autophagy modulates the cellular response to the microenvironment changes.
{"title":"Autophagy in the endothelium commands flow-mediated vascular reactivity and remodelling, and regulates VEGFR2 subcellular localization and signalling","authors":"Pierre-Louis Tharaux, Olivia Lenoir","doi":"10.1080/27694127.2023.2277585","DOIUrl":"https://doi.org/10.1080/27694127.2023.2277585","url":null,"abstract":"Pharmacological approaches aimed at increasing autophagic flux and genetically engineered mice with autophagy deficiency in the endothelium have demonstrated that autophagy exerts vessel protection against metabolic stresses and vascular aging. However, the identity of the specific cellular processes that autophagy controls in endothelial cells remained unclear. In this punctum, we discuss our recent findings on the multiple functions of autophagy in the endothelium. Particularly, we highlighted that autophagy controls flow-mediated vascular reactivity and remodeling. We have also focused on the role of autophagy machinery in regulating protein distribution within the cell and on the results demonstrating how autophagy modulates the cellular response to the microenvironment changes.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"38 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"136347006","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}
Pub Date : 2023-11-10DOI: 10.1080/27694127.2023.2277582
Nobuo N. Noda
Atg8 and Atg12 are ubiquitin-like proteins, conjugated to phosphatidylethanolamine (PE) and Atg5, respectively, through enzymatic reactions similar to ubiquitylation. The resultant Atg8–PE and Atg12–Atg5 conjugates play crucial roles in autophagy. Structural studies have been extensively performed on all Atg proteins (Atg3, Atg4, Atg5, Atg7, Atg8, Atg10, Atg12, Atg16) involved in these conjugation systems. This review summarizes structural studies and discusses mechanisms of conjugation and deconjugation reactions, as well as autophagic functions of the Atg8 and Atg12 conjugation systems.
{"title":"Structural biology of the Atg8 and Atg12 conjugation systems","authors":"Nobuo N. Noda","doi":"10.1080/27694127.2023.2277582","DOIUrl":"https://doi.org/10.1080/27694127.2023.2277582","url":null,"abstract":"Atg8 and Atg12 are ubiquitin-like proteins, conjugated to phosphatidylethanolamine (PE) and Atg5, respectively, through enzymatic reactions similar to ubiquitylation. The resultant Atg8–PE and Atg12–Atg5 conjugates play crucial roles in autophagy. Structural studies have been extensively performed on all Atg proteins (Atg3, Atg4, Atg5, Atg7, Atg8, Atg10, Atg12, Atg16) involved in these conjugation systems. This review summarizes structural studies and discusses mechanisms of conjugation and deconjugation reactions, as well as autophagic functions of the Atg8 and Atg12 conjugation systems.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" 22","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135141882","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}
The caspase-like protease MALT1 promotes immune responses and oncogenesis in mammals by activating the transcription factor NF-κB. MALT1 is remarkably conserved from mammals to simple metazoans devoid of NF-κB homologs, like the nematode C. elegans. To discover more ancient, NF-κB -independent MALT1 functions, we analysed the phenotype of C. elegans upon silencing of MALT-1 expression systemically or in a tissue-specific manner. MALT-1 silencing in the intestine caused a significant increase in life span, whereas intestinal overexpression of MALT-1 shortened life expectancy. Interestingly, MALT-1-deficient animals showed higher constitutive levels of autophagy in the intestine, which were particularly evident in aged or starved nematodes. Silencing of the autophagy regulators ATG-13, BEC-1 or LGG-2, but not the TOR homolog LET-363, reversed lifespan extension caused by MALT-1 deficiency. These findings suggest that MALT-1 limits the lifespan of C. elegans by acting as an inhibitor of an early step of autophagy in the intestine.
{"title":"MALT-1 shortens lifespan by inhibiting autophagy in the intestine of <i>C. elegans</i>","authors":"Julie Vérièpe-Salerno, Silvia Podavini, Marcus J.C. Long, Irina Kolotuev, Muriel Cuendet, Margot Thome","doi":"10.1080/27694127.2023.2277584","DOIUrl":"https://doi.org/10.1080/27694127.2023.2277584","url":null,"abstract":"The caspase-like protease MALT1 promotes immune responses and oncogenesis in mammals by activating the transcription factor NF-κB. MALT1 is remarkably conserved from mammals to simple metazoans devoid of NF-κB homologs, like the nematode C. elegans. To discover more ancient, NF-κB -independent MALT1 functions, we analysed the phenotype of C. elegans upon silencing of MALT-1 expression systemically or in a tissue-specific manner. MALT-1 silencing in the intestine caused a significant increase in life span, whereas intestinal overexpression of MALT-1 shortened life expectancy. Interestingly, MALT-1-deficient animals showed higher constitutive levels of autophagy in the intestine, which were particularly evident in aged or starved nematodes. Silencing of the autophagy regulators ATG-13, BEC-1 or LGG-2, but not the TOR homolog LET-363, reversed lifespan extension caused by MALT-1 deficiency. These findings suggest that MALT-1 limits the lifespan of C. elegans by acting as an inhibitor of an early step of autophagy in the intestine.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" 2","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135242845","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}
Pub Date : 2023-11-09DOI: 10.1080/27694127.2023.2278299
Yuchieh Jay Lin, Guang-Chao Chen
The ubiquitin-proteasome system (UPS) and autophagy are highly conserved processes that maintain cellular health through the clearance of misfolded/aberrant proteins and damaged organelles. Ubiquitination is a crucial protein modification to regulate entry in these two pathways. However, the function of deubiquitinases (DUBs) in the UPS and autophagy remains largely unclear. The Leon/USP5 deubiquitinase is essential for maintaining ubiquitin homeostasis and proteasome function. In our recent study, we found that Leon/USP5 depletion resulted in the induction of autophagosome formation and an enhancement of the autophagic flux. Additionally, a genetic analysis in Drosophila revealed that Leon overexpression suppressed Atg1-induced cell death. We further showed that Leon/USP5 interacts with the autophagy initiator Atg1/ULK1, regulating its levels and thus modulating autophagosome formation. These findings suggest that Leon/USP5 plays a dual role in regulation of UPS and autophagy.
{"title":"Dual function of the Leon/USP5 deubiquitinase in the ubiquitin-proteasome and autophagic pathways","authors":"Yuchieh Jay Lin, Guang-Chao Chen","doi":"10.1080/27694127.2023.2278299","DOIUrl":"https://doi.org/10.1080/27694127.2023.2278299","url":null,"abstract":"The ubiquitin-proteasome system (UPS) and autophagy are highly conserved processes that maintain cellular health through the clearance of misfolded/aberrant proteins and damaged organelles. Ubiquitination is a crucial protein modification to regulate entry in these two pathways. However, the function of deubiquitinases (DUBs) in the UPS and autophagy remains largely unclear. The Leon/USP5 deubiquitinase is essential for maintaining ubiquitin homeostasis and proteasome function. In our recent study, we found that Leon/USP5 depletion resulted in the induction of autophagosome formation and an enhancement of the autophagic flux. Additionally, a genetic analysis in Drosophila revealed that Leon overexpression suppressed Atg1-induced cell death. We further showed that Leon/USP5 interacts with the autophagy initiator Atg1/ULK1, regulating its levels and thus modulating autophagosome formation. These findings suggest that Leon/USP5 plays a dual role in regulation of UPS and autophagy.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":" 21","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135242848","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}
Pub Date : 2023-11-05DOI: 10.1080/27694127.2023.2278120
Alessandra Romagnoli, Martina Di Rienzo, Mauro Piacentini, Gian Maria Fimia
Mycobacterium tuberculosis (Mtb) promotes its intracellular persistence by subverting defense mechanisms, such as autophagy. Remarkably, enhancing autophagy is sufficient to trigger intracellular Mtb killing and effective immune response, making this process a valid target of host-directed therapies. However, several aspects of autophagy regulation during Mtb infection remain unsolved. Tripartite motif (TRIM) proteins are a large family of ubiquitin ligases primarily involved in innate immunity by regulating inflammation and autophagy. By combining transcriptomic and infectivity screens, we recently identified a set of TRIMs that modulate Mtb replication. In detail, overexpression of TRIM22 and TRIM32 reduces Mtb growth in THP1 macrophages, while that of TRIM36 and TRIM56 promotes Mtb replication. Analysis of the molecular mechanisms underlying inhibition of Mtb replication by TRIM32 showed that its overexpression promote xenophagy, a selective autophagy of pathogens, by increasing Mtb ubiquitination and the recruitment of CALCOCO2/NDP52 (calcium binding and coiled-coil domain 2) and MAP1LC3B (microtubule-associated protein 1 light chain 3B) to intracellular bacteria. Consistently, TRIM32 downregulation reduces the xenophagic response, resulting in increased Mtb replication. Altogether, we characterized a novel role for TRIM32 in the host response to pathogen infections and identify TRIM36 and TRIM56 as possible host factors required for Mtb infection.
{"title":"TRIMming down Mycobacterium tuberculosis replication: TRIM32 is required for bacterial ubiquitination and autophagy induction in macrophages","authors":"Alessandra Romagnoli, Martina Di Rienzo, Mauro Piacentini, Gian Maria Fimia","doi":"10.1080/27694127.2023.2278120","DOIUrl":"https://doi.org/10.1080/27694127.2023.2278120","url":null,"abstract":"Mycobacterium tuberculosis (Mtb) promotes its intracellular persistence by subverting defense mechanisms, such as autophagy. Remarkably, enhancing autophagy is sufficient to trigger intracellular Mtb killing and effective immune response, making this process a valid target of host-directed therapies. However, several aspects of autophagy regulation during Mtb infection remain unsolved. Tripartite motif (TRIM) proteins are a large family of ubiquitin ligases primarily involved in innate immunity by regulating inflammation and autophagy. By combining transcriptomic and infectivity screens, we recently identified a set of TRIMs that modulate Mtb replication. In detail, overexpression of TRIM22 and TRIM32 reduces Mtb growth in THP1 macrophages, while that of TRIM36 and TRIM56 promotes Mtb replication. Analysis of the molecular mechanisms underlying inhibition of Mtb replication by TRIM32 showed that its overexpression promote xenophagy, a selective autophagy of pathogens, by increasing Mtb ubiquitination and the recruitment of CALCOCO2/NDP52 (calcium binding and coiled-coil domain 2) and MAP1LC3B (microtubule-associated protein 1 light chain 3B) to intracellular bacteria. Consistently, TRIM32 downregulation reduces the xenophagic response, resulting in increased Mtb replication. Altogether, we characterized a novel role for TRIM32 in the host response to pathogen infections and identify TRIM36 and TRIM56 as possible host factors required for Mtb infection.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"61 10","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135726256","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}
Pub Date : 2023-10-23DOI: 10.1080/27694127.2023.2271281
Takashi Kikuma, Joichiro Nishio
There are two types of autophagy, non-selective (bulk) autophagy, in which substrates are randomly incorporated into autophagosomes, and selective autophagy, in which substrates are specifically targeted. In filamentous fungi, the molecular mechanism underlying selective autophagy remains largely unknown. Recently we identified a novel protein, AoAtg8-interacting protein A (AeiA), in the filamentous fungus Aspergillus oryzae. AeiA was localized to peroxisomes and autophagosomal intermediates, such as phagophore assembly site (PAS) and the phagophore. Moreover, pexophagy flux was reduced in AeiA deletants. Taken together, AeiA is a novel selective autophagy-related protein that contributes to pexophagy in A. oryzae. Our findings provide insight into the molecular mechanisms of selective autophagy including pexophagy in filamentous fungi. Abbreviations: AIM, Atg8-family interacting motifs; Atg8, autophagy-related 8; EGFP, enhanced green fluorescent protein; GABARAP, Gamma aminobutyric acid A receptor associated protein; LC3, Microtubule-associated protein light chain 3; MTS, microbody targeting signal; PD, potato dextrose.
{"title":"AeiA, an Atg8-interacting protein in <i>Aspergillus oryzae</i> , promotes peroxisome degradation by pexophagy","authors":"Takashi Kikuma, Joichiro Nishio","doi":"10.1080/27694127.2023.2271281","DOIUrl":"https://doi.org/10.1080/27694127.2023.2271281","url":null,"abstract":"There are two types of autophagy, non-selective (bulk) autophagy, in which substrates are randomly incorporated into autophagosomes, and selective autophagy, in which substrates are specifically targeted. In filamentous fungi, the molecular mechanism underlying selective autophagy remains largely unknown. Recently we identified a novel protein, AoAtg8-interacting protein A (AeiA), in the filamentous fungus Aspergillus oryzae. AeiA was localized to peroxisomes and autophagosomal intermediates, such as phagophore assembly site (PAS) and the phagophore. Moreover, pexophagy flux was reduced in AeiA deletants. Taken together, AeiA is a novel selective autophagy-related protein that contributes to pexophagy in A. oryzae. Our findings provide insight into the molecular mechanisms of selective autophagy including pexophagy in filamentous fungi. Abbreviations: AIM, Atg8-family interacting motifs; Atg8, autophagy-related 8; EGFP, enhanced green fluorescent protein; GABARAP, Gamma aminobutyric acid A receptor associated protein; LC3, Microtubule-associated protein light chain 3; MTS, microbody targeting signal; PD, potato dextrose.","PeriodicalId":72341,"journal":{"name":"Autophagy reports","volume":"56 8","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135413303","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}
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