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ProteomicsRsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress
The heat-shock response is a complex cellular program that induces major changes in protein translation, folding and degradation to alleviate toxicity caused by protein misfolding. While heat-shock has been widely used to study proteostasis, it remained unclear how misfolded proteins are targeted fo...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-07-06 | PXD001214 | Pride
Rsp5 Heat-shock Cytosolic protein quality control 
ProteomicsDeubiquitinase activity is required for the degradation of misfolded cytosolic proteins upon heat-stress
Elimination of misfolded proteins is crucial for proteostasis and to prevent proteinopathies. Nedd4/Rsp5 emerged as a major E3 ligase involved in multiple quality control pathways that target misfolded plasma membrane proteins, aggregated polypeptides, and cytosolic heat-induced misfolded proteins f...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-03-01 | PXD004747 | Pride
Deubiquitinase Cytosolic protein quality control Heat stress 
ProteomicsMisfolded SOD1 binds the ubiquitin ligase TRAF6
Amyotrophic lateral sclerosis (ALS) is a fatal disease, characterized by the selective loss of motor neurons. Mutations in Cu/Zn superoxide dismutase (SOD1) are the second most common cause of ALS and it is now well accepted that they result in a gain of toxicity due to protein misfolding. We previo...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-02-24 | PXD015279 | Pride
Tnf receptor-associated factor 6 (traf6) Superoxide dismutase 1 (sod1) Mitochondria Protein misfolding Ubiquitin Amyotrophic lateral sclerosis (als) Aggregation 
GenomicsHematopoietic Stem Cells Preferentially Traffic Misfolded Proteins to Aggresomes and Depend on Aggrephagy to Maintain Protein Homeostasis
Hematopoietic Stem Cells Preferentially Traffic Misfolded Proteins to Aggresomes and Depend on Aggrephagy to Maintain Protein Homeostasis
PRJNA848853 | ENA
TranscriptomicsConstitutive expression of misfolded surfactant protein C
Mutations in the gene encoding surfactant protein C (SFTPC) have been linked to interstitial lung disease in children and adults. Expression of the index mutation, SP-Cdeltaexon4, in transiently transfected cells and type II cells of transgenic mice resulted in misfolding of the proprotein, activati...
ORGANISM(S): Homo sapiens 
2006-03-20 | GSE2980 | GEO
TranscriptomicsCytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast
Cells maintain proteostasis by selectively recognizing and targeting misfolded proteins for degradation. In Saccharomyces cerevisiae, the Hsp70 nucleotide exchange factor Fes1 is essential for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system. Here we show...
ORGANISM(S): Saccharomyces cerevisiae 
2016-02-29 | E-GEOD-78136 | biostudies-arrayexpress
ProteomicsThe mechanism to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes
Endoplasmic reticulum (ER)-associated degradation (ERAD) and ER-phagy are two principal degradative mechanisms in the ER; however, the crosstalk between these two pathways and its physiological significance remain unexplored. Here we report that SEL1L-HRD1 ERAD limits autophagy and that, when ERAD i...
ORGANISM(S): Mus musculus (Mouse) 
2023-04-25 | PXD040899 | Pride
Autophagy Lipoprotein lipase Tryptophan loop Sel1l-hrd1 erad Cerfs Bip Er-phagy Protein aggregation Phase separation Soluble-to-insoluble phase transition 
UnknownDiverse Misfolded Conformational Strains and Cross-seeding of Misfolded Proteins Implicated in Neurodegenerative Diseases.
Not available
S-EPMC6629833 | biostudies-literature
TranscriptomicsCytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast
Cells maintain proteostasis by selectively recognizing and targeting misfolded proteins for degradation. In Saccharomyces cerevisiae, the Hsp70 nucleotide exchange factor Fes1 is essential for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system. Here we show...
ORGANISM(S): Saccharomyces cerevisiae 
2016-02-29 | GSE78136 | GEO
UnknownEnhanced Degradation of Misfolded Proteins Promotes Tumorigenesis.
Not available
S-EPMC5603913 | biostudies-literature
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