GPMDB00225OtherWalther DM, et al.InstrumentNot AvailableNot availableWorm, 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2310019637http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019758http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019751http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019630http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019752http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019631http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019750http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019755http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019634http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019756http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019635http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019753http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019632http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019754http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019633Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, et al.Not availableGPMDBAging has been associated with a progressive decline of proteostasis, but how this process affects proteome composition remains largely unexplored. Here, we profiled more than 5,000 proteins along the lifespan of the nematode C. elegans. We find that one-third of proteins change in abundance at least 2-fold during aging, resulting in a severe proteome imbalance. These changes are reduced in the long-lived daf-2 mutant but are enhanced in the short-lived daf-16 mutant. While ribosomal proteins decline and lose normal stoichiometry, proteasome complexes increase. Proteome imbalance is accompanied by widespread protein aggregation, with abundant proteins that exceed solubility contributing most to aggregate load. Notably, the properties by which proteins are selected for aggregation differ in the daf-2 mutant, and an increased formation of aggregates associated with small heat-shock proteins is observed. We suggest that sequestering proteins into chaperone-enriched aggregates is a protective strategy to slow proteostasis decline during nematode aging.Widespread Proteome Remodeling and Aggregation in Aging C. elegans.Walther Dirk M DM,Kasturi Prasad P,Zheng Min M,Pinkert Stefan S,Vecchi Giulia G,Ciryam Prajwal P,Morimoto Richard I RI,Dobson Christopher M CM,Vendruscolo Michele M,Mann Matthias M,Hartl F Ulrich FU,Walther Dirk M DM, Kasturi Prasad P, Zheng Min M, Pinkert Stefan S, Vecchi Giulia G, Ciryam Prajwal P, Morimoto Richard I RI, Dobson Christopher M CM, Vendruscolo Michele M, Mann Matthias M, Hartl F Ulrich FUageing, Senescence, Biological Aging, Aging, BIOL AGING, Proteomes, Biological, AGING BIOL.Senescence, data, Nemata, lifespan, cell, entire lifespan, Ass-1, entire life cycle, life, Proteins, Gene, proteins, Aging, Cell, Protein Gene Products, ASS, Gene Proteins, polypeptide, roundworm, ageing, nematode, Biological Aging, Experiment, Biological, AA408052, Protein, nematodes, AGING BIOL, Proteomes., roundworms, Gene Products, fold, BIOL AGING, Rhabditis elegansageing, Senescence, Biological Aging, Aging, BIOL AGING, Proteomes, Biological, AGING BIOL.projections, Solubilities, lifespan, Stress Proteins, lamellae, Ass-1, Protein Homeostasis, Gene, Ribosomal Protein, biosynthesis, Aging, composed of, process of organ, supernumerary, protrusion, lamella, reduced, Biological, subnumerary, AA408052, AGING BIOL, Gene Products, fold, slow, tiny, present in fewer numbers in organism, multicellular organismal biosynthetic process, Normalities, average, Senescence, increased, Ribosomal, single-organism biosynthetic process, Heat Shock Proteins, formation, entire lifespan, entire life cycle, anabolism, long, N, hypoplasia, stubby, Homeostases, composition, proteins, ridges, decreased number, retention, Proteostases, synthesis, ASS, roundworm, Biological Aging, nematode, decreased, DAF, papilla, nematodes, roundworms, CR, TC, 26S proteasome, associated, laminae, small, Nemata, anatomical protrusion, anatomical process, Heat Shock Protein, Protein Homeostases, Proteins, lamina, CROM, flanges, Normalcy, compositionality, polypeptide, shortened, Protein, shelf, Heat-Shock Protein, BIOL AGING, Rhabditis elegans, flange, organ process, slow speed, proteasome, Homeostasis, maintenance of localization, underdeveloped, Normality, storage, increased number, shelves, content, life, AGING BIOL., projection, ridge, Protein Gene Products, ageing, process, processes, Gene Proteins, present in greater numbers in organism, Health, spine, structure, processus, sequestering, short, Proteomes, accessory2205http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310019629dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0067859346082665020.01.0falseWidespread Proteome Remodeling and Aggregation in Aging C. elegans.Data from ProteomeXchange, PXD ID: PXD001364. Experiment: AggregatesSILAC_DAF16_D01, file: 20110921_Velos3_DiWa_SA_Celegans_AggregatesSILAC_DAF16_D01-3.mzml. Published as part of Cell. 2015 May 7;161(4):919-932 . From the Abstract: {{i}} ... Here, we profiled more than 5, 000 proteins along the lifespan of the nematode C. elegans. We find that one-third of proteins change in abundance at least 2-fold during aging, resulting in a severe proteome imbalance ... {{/i}}2015-05-14GPM3231001962925957690PXD001364PXD001364