{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Swords SB"],"funding":["National Institute of Neurological Disorders and Stroke","NINDS NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["792-808"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11062384"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(4)"],"pubmed_abstract":["Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autophagic lysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining lysosomal capacity is required to maintain cellular health, especially in neurons where lysosomal dysfunction has been repeatedly implicated in neurodegenerative disease. The DNA-J domain HSC70 co-chaperone RME-8/DNAJC13 has been linked to endosomal coat protein regulation and to neurological disease. We report new analysis of the requirements for the RME-8/DNAJC13 protein in neurons, focusing on intact <i>C. elegans</i> mechanosensory neurons, and primary mouse cortical neurons in culture. Loss of RME-8/DNAJC13 in both systems results in ac"],"journal":["Autophagy"],"pubmed_title":["A conserved requirement for RME-8/DNAJC13 in neuronal autophagic lysosome reformation."],"pmcid":["PMC11062384"],"funding_grant_id":["F31 NS117034","R01 NS089737","5R01GM135326","R01 GM135326","5R01NS089737","F31NS117034"],"pubmed_authors":["Modi J","Cai Q","Jia N","Norris A","Swords SB","Grant BD"],"additional_accession":[]},"is_claimable":false,"name":"A conserved requirement for RME-8/DNAJC13 in neuronal autophagic lysosome reformation.","description":"Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autophagic lysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining lysosomal capacity is required to maintain cellular health, especially in neurons where lysosomal dysfunction has been repeatedly implicated in neurodegenerative disease. The DNA-J domain HSC70 co-chaperone RME-8/DNAJC13 has been linked to endosomal coat protein regulation and to neurological disease. We report new analysis of the requirements for the RME-8/DNAJC13 protein in neurons, focusing on intact <i>C. elegans</i> mechanosensory neurons, and primary mouse cortical neurons in culture. Loss of RME-8/DNAJC13 in both systems results in ac","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-07-16T15:04:58.15Z","creation":"2025-04-04T14:40:28.429Z"},"accession":"S-EPMC11062384","cross_references":{"pubmed":["37942902"],"doi":["10.1080/15548627.2023.2269028"]}}