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ProteomicsCHN-1 and CHN-1 L141R interacting proteins
Proteostasis is achieved by quality control pathways that support the generation of correctly folded proteins, prevent protein misfolding and remove toxic proteins. The quality control E3 ligase CHIP ubiquitylates damaged proteins consigned by chaperone partners for disposal through the endo-lysosom...
ORGANISM(S): Caenorhabditis elegans 
2022-08-25 | PXD025375 | Pride
C.elegans Lc-ms/ms 
ProteomicsThermosensation is linked to ubiquitin-dependent protein turnover via insulin and calcineurin signalling
Organismal physiology and survival are influenced by environmental conditions and linked to protein quality control. Proteome integrity is achieved by maintaining an intricate balance between protein folding and degradation. In Caenorhabditis elegans, acute heat stress determines cell non-autonomous...
ORGANISM(S): Caenorhabditis elegans 
2022-08-12 | PXD016676 | Pride
Calcineurin signaling Ciliated neurons Proteostasis Ageing Insulin signaling Ubiquitin Aggregation 
ProteomicsReprograming of Proteasomal Degradation by Branched Chain Amino Acid Metabolism
Branched chain amino acids (BCAAs) play an important role in energy and protein regulation. Defects in BCAA metabolism are linked to numerous pathologies, including diabetes, neurodegeneration, and premature aging. Isovaleric acidemia is a metabolic disease caused by defective leucine breakdown and ...
ORGANISM(S): Caenorhabditis elegans 
2022-09-22 | PXD028286 | Pride
C. elegans  ubiquitin  leucine catabolism  branched chain amino acid (bcaa)  bcat  ivd  isovaleric acidemia 
ProteomicsProteomic analysis of mitoUFD binding partners
This project is to identify the binding partners of the OMM anchored ubiquitin-fusion degradation substrate (mitoUFD) in comparison with the mitoGFP control that lacks the ubiquitin fusion as the degradation signal. In addition, we performed RNAi knockdown for bcat-1, lars-1 and gcn-2 compared to th...
ORGANISM(S): Caenorhabditis elegans 
2025-11-05 | PXD062734 | Pride
Mitochondria  outer mitochondrial membrane  mitoufd  pulldown 
ProteomicsProteomics after co-immunoprecipitation of myosin/MHC B/UNC-54 (with a Gly387Arg mutation) from C. elegans worms grown on nhl-1 or F40A3.6 RNAi compared to control RNAi
This project includes 20 samples after immunoprecipitation of C. elegans myosin heavy chain B (MHC B/UNC-54/F11C3.3, UniProt P02566 with a Gly387Arg mutation) in 4 replicates of 4 conditions. Lysates from a myosin-misfolding C. elegans strain (unc-54(e1301) with a Gly387Arg substitution in MHC B) gr...
ORGANISM(S): Caenorhabditis elegans 
2024-07-16 | PXD045076 | Pride
Myosin C. elegans Co-immunoprecipitation Rnai Interactome Muscle 
ProteomicsWhole worm proteomics after optogenetically induced mechanical muscle stress (OptIMMuS)
This project includes 16 samples of transgenic C. elegans whole worm lysate after mechanical stress in 4 replicates of 4 conditions. Transgenic C. elegans strains expressing the optogenetic channelrhodopsin mutant ChR2(C128S;H134R)-FLAG in body wall muscle cells (PP3189 hhIs251[myo-3p::ChR2(C128S,H1...
ORGANISM(S): Caenorhabditis elegans 
2024-07-16 | PXD045078 | Pride
C. elegans Optogenetics Mechanical stress Muscle 
ProteomicsProteomics after labeling the vicinity of UNC-45 using miniTurbo and TurboID biotin ligases followed by streptavidin pull-down under non-stress and optogenetically induced mechanical muscle stress (OptIMMuS).
This project includes two proximity labeling experiments, one to establish the vicinity of UNC-45 under non-stress conditions and one to examine changes in the vicinity of UNC-45 under optogenetically induced mechanical muscle stress. The first non-stress experiment consists of 15 samples after biot...
ORGANISM(S): Caenorhabditis elegans 
2024-07-16 | PXD045081 | Pride
C. elegans Optogenetics Unc-45 Proximity labelling Mechanical stress Muscle 
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