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ProteomicsProteomic characterization of Hsp78-interacting proteins highlights chaperone role during protein aggregation in mitochondria under heat stress - Part A Protein Interactions
Chaperones of the Hsp100 chaperone family support protein homeostasis, the maintenance of protein activity under stress, by refolding aggregated proteins or targeting them for degradation. Hsp78, the ClpB-type mitochondrial member of the Hsp100 family, can be found in lower eukaryotes like yeast. Al...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-09-20 | PXD030405 | Pride
Yeast  cell biology  mitochondria  heat stress  protein aggregation  proteostasis  chaperone  hsp78 
ProteomicsProteomic characterization of Hsp78-interacting proteins highlights chaperone role during protein aggregation in mitochondria under heat stress - Part B Aggregation
Chaperones of the Hsp100 chaperone family support protein homeostasis, the maintenance of protein activity under stress, by refolding aggregated proteins or targeting them for degradation. Hsp78, the ClpB-type mitochondrial member of the Hsp100 family, can be found in lower eukaryotes like yeast. Al...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-09-20 | PXD030436 | Pride
Hsp78 Yeast Cell biology Mitochondria Chaperone Protein aggregation Proteostasis Heat stress 
ProteomicsProteomic analysis of the role of the quality control protease LONP1 in mitochondrial protein aggregation
The mitochondrial matrix protease LONP1 is an essential part of the organellar protein quality control system. LONP1 has been shown to be involved in respiration control and apoptosis. Furthermore, a reduction in LONP1 level correlates with ageing processes. Up to now, the effects of a LONP1 defect ...
ORGANISM(S): Homo sapiens (Human) 
2022-01-31 | PXD026941 | Pride
Human Protein aggregation Heat stress Lonp1 atp-dependent protease Mitochondria Genetic alteration via crispr/cas Protein degradation 
ProteomicsPrevention of mitochondrial proteotoxicity by formation of a chaperone-dependent protective shell around aggregated polypeptides
The potential proteotoxicity of mitochondrial aggregates in yeast cells is reduced by a sequestration of affected polypeptides into a mitochondrial protein quality control compartment (IMiQ). Based on the expression of an aggregation-prone protein in the mitochondrial matrix, we determined the effec...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-08-21 | PXD059828 | Pride
Mitochondria Hsp70 Chaperone Protein aggregation Proteostasis Yeast 
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