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ProteomicsLONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
Because 99% of the mitochondrial proteome is encoded by the nucleus, most mitochondrial precursor polypeptides are imported from the cytosol into the mitochondrion, where they must efficiently fold into their functional state. Mitochondrial precursors are imported as unfolded polypeptides due to th...
ORGANISM(S): Homo sapiens (Human) 
2020-12-07 | PXD021939 | Pride
Aggregates Protein homeostasis Mitochondria Human 
ProteomicsTurboID-based proximity labeling to identify LONP1-targeting proteins
It is documented that intracellular succinate levels are maintained and regulated by mitochondrial complexes II. In order to define the LONP1-dependent regulators of succinate content, unbiased TurboID-based proximity labeling was employed to exploit LONP1-targeting proteins. Our results showed that...
ORGANISM(S): Homo sapiens (Human) 
2023-04-08 | PXD031197 | Pride
Lonp1 Human Turboid 
ProteomicsQuantitative proteomics analysis of liver from LONP1 Knockout mice
The mechanisms of hepatic stellate cell (HSC) activation and the development of liver fibrosis remains largely unknow. Here, we revealed a fibrosis related mechanism of hepatocytes-HSCs crosstalk regulated by hepatocyte LONP1. We demonstrate that hepatocyte LONP1 expression is decreased in HFD-fed m...
ORGANISM(S): Mus musculus (Mouse) 
2025-09-23 | PXD055467 | Pride
Lonp1  hepatic stellate cell  liver fibrosis  orotic acid 
GenomicsRNAseq analysis of skeletal muscle transcriptomes from wild-type and LONP1 skeletal muscle specific knockout (LONP1-MKO) mice
RNAseq analysis of skeletal muscle transcriptomes from wild-type and LONP1 skeletal muscle specific knockout (LONP1-MKO) mice
PRJNA699182 | ENA
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 
GenomicsGenome-wide mapping of H3K4me1 status in primary adipocytes isolated from wild-type (WT) and Lonp1-knockout (LONP1 AKO) mice
Genome-wide mapping of H3K4me1 status in primary adipocytes isolated from wild-type (WT) and Lonp1-knockout (LONP1 AKO) mice
PRJNA922196 | ENA
ProteomicsiTRAQ-based analysis of muscle mitochondria isolated from LONP1-mKO mice
This experiment was conducted to identify the mitochondrial protein changes in the presence and absence of LONP1 in skeletal muscle. The following abstract from the submitted manuscript describes the major findings of this work.Disuse-associated loss of muscle LONP1 impairs mitochondrial quality and...
ORGANISM(S): Mus musculus (Mouse) 
2022-01-05 | PXD029722 | Pride
Mouse Skeletal muscle 
TranscriptomicsRNAseq analysis of skeletal muscle transcriptomes from wild-type and LONP1 skeletal muscle specific knockout (LONP1-MKO) mice
Mitochondria serve diverse functions and are essential organelles that require continuous surveillance to maintaintheir integrity and function. LONP1 is an evolutionarily conservedserine peptidase that safeguards mitochondrial protein quality from yeast to human.To investigatethe physiological role ...
ORGANISM(S): Mus musculus 
2022-01-05 | GSE166071 | GEO
GenomicsRNAseq analysis of skeletal muscle transcriptomes from wild-type, LONP1 skeletal muscle specific knockout (LONP1 mKO) and LONP1ATF4 skeletal muscle double-knockout (LONP1ATF4 DmKO) mice.
RNAseq analysis of skeletal muscle transcriptomes from wild-type, LONP1 skeletal muscle specific knockout (LONP1 mKO) and LONP1ATF4 skeletal muscle double-knockout (LONP1ATF4 DmKO) mice.
PRJNA794074 | ENA
UnknownLONP1 de novo dominant mutation causes mitochondrial encephalopathy with loss of LONP1 chaperone activity and excessive LONP1 proteolytic activity.
Not available
S-EPMC8628847 | biostudies-literature
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