{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wu H"],"funding":["National Research Foundation Singapore (National Research Foundation-Prime Minister's office, Republic of Singapore)","A*STAR | Singapore Institute of Manufacturing Technology (Singapore Institute of Manufacturing Technology - A STAR)","Ministry of Education - Singapore (MOE)","Ministry of Education - Singapore","National Research Foundation Singapore","A*STAR | Singapore Institute of Manufacturing Technology"],"pagination":["9026"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11489672"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Protein aggregation plays key roles in age-related degenerative diseases, but how different proteins coalesce to form inclusions that vary in composition, morphology, molecular dynamics and confer physiological consequences is poorly understood. Here we employ a general reporter based on mutant Hsp104 to identify proteins forming aggregates in human cells under common proteotoxic stress. We identify over 300 proteins that form different inclusions containing subsets of aggregating proteins. In particular, TDP43, implicated in Amyotrophic Lateral Sclerosis (ALS), partitions dynamically between two distinct types of aggregates: stress granule and a previously unknown non-dynamic (solid-like) inclusion at the ER exit sites (ERES). TDP43-ERES co-aggregation is induced by diverse proteotoxic st"],"journal":["Nature communications"],"pubmed_title":["TDP43 aggregation at ER-exit sites impairs ER-to-Golgi transport."],"pmcid":["PMC11489672"],"funding_grant_id":["NRF-SIS \"SingMass\"","NRF-MSG-2023-0001","NRF-SIS “SingMass”","A-0007081-00-00"],"pubmed_authors":["Gupta R","Ostrow LW","Zhu J","Wang LC","Sow BM","Leow D","Yeo CJJ","Wilsbach K","Sobota RM","Li R","Gallo KM","Wu H"],"additional_accession":[]},"is_claimable":false,"name":"TDP43 aggregation at ER-exit sites impairs ER-to-Golgi transport.","description":"Protein aggregation plays key roles in age-related degenerative diseases, but how different proteins coalesce to form inclusions that vary in composition, morphology, molecular dynamics and confer physiological consequences is poorly understood. Here we employ a general reporter based on mutant Hsp104 to identify proteins forming aggregates in human cells under common proteotoxic stress. We identify over 300 proteins that form different inclusions containing subsets of aggregating proteins. In particular, TDP43, implicated in Amyotrophic Lateral Sclerosis (ALS), partitions dynamically between two distinct types of aggregates: stress granule and a previously unknown non-dynamic (solid-like) inclusion at the ER exit sites (ERES). TDP43-ERES co-aggregation is induced by diverse proteotoxic st","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T05:37:50.335Z","creation":"2025-04-04T22:47:25.746Z"},"accession":"S-EPMC11489672","cross_references":{"pubmed":["39424779"],"doi":["10.1038/s41467-024-52706-7"]}}