Refine
Year of publication
Language
- English (62)
Has Fulltext
- yes (62)
Is part of the Bibliography
- no (62)
Keywords
- Proteomics (3)
- complexome profiling (3)
- mitochondria (3)
- Aging (2)
- Calpain (2)
- Complex I (2)
- NADPH oxidase (2)
- Podospora anserina (2)
- Reactive oxygen species (2)
- aging (2)
- bioenergetics (2)
- long non-coding RNA (2)
- mitochondrial disease (2)
- A/D transition (1)
- AAA+ disaggregase (1)
- Activities of daily living (1)
- Adult neurogenesis (1)
- Alternative oxidase (1)
- Apoptosis (1)
- Ataxia (1)
- Autoimmune vasculopathy (1)
- Autophagy (1)
- BIAM switch assay (1)
- BIAM-switch (1)
- BPTF (1)
- Behavior (1)
- Biochemistry (1)
- Brain (1)
- Calcium calmodulin kinase (1)
- Cardiac infarction (1)
- Cardiology (1)
- Cardiomyopathy (1)
- Cell signalling (1)
- Chaperone (1)
- Chemical modification (1)
- Chemiluminescence (1)
- ClpB (1)
- Complex II (1)
- Complexome profiling (1)
- Conformational change (1)
- Cortex (1)
- DNA Damage (1)
- DNA methylation (1)
- Data visualization (1)
- Database (1)
- ERAL1 (1)
- Endothelial cell (EC) (1)
- Endothelial cells (1)
- Endothelial protein C receptor (1)
- FAIR (1)
- Flavin mononucleotide (1)
- G3BP1 (1)
- HARS2 (1)
- HSP (hereditary spastic paraplegia) (1)
- Heart (1)
- Heart transplantation (1)
- Hig1 (1)
- Hypoxia inducible factor (1)
- ICAM-1 (1)
- IL-1β (1)
- Innate immunity (1)
- IntelliCage (1)
- Isoforms (1)
- KLHL11 (1)
- LARS2 (1)
- Lactic acidosis (1)
- Leukodystrophy (1)
- LncRNA - long noncoding RNA (1)
- Long non-coding RNAs (1)
- Lucigenin (1)
- Lysosome (1)
- MEIS homeodomain protein (1)
- MTRNR1 (1)
- Mass spectrometry (1)
- Membrane assays (1)
- Microparticles (1)
- Mitochondria (1)
- Mitochondrial ROS (1)
- Mitochondrial amino acid tRNA synthetases (1)
- Mitochondrial complex I (1)
- Mitochondrial disease (1)
- Mitochondrial disorder (1)
- Mitochondrial dysfunction (1)
- N-hydroxysuccinimide (1)
- N471D strumpellin knock-in mice (1)
- NADH:ubiquinone oxidoreductase (1)
- NDUFA6 (1)
- NDUFAF8 (1)
- NURF (1)
- Neonatal (1)
- Neurodegeneration (1)
- Nitric oxide (1)
- Nox (1)
- Nox4 (1)
- OXPHOS (1)
- POLG (1)
- PRLTS3 (1)
- Parkinson’s disease (1)
- Perrault syndrome (1)
- Play (1)
- Pleasure (1)
- Post-translational modifications (1)
- Posttranslational modification (1)
- Prognosis (1)
- Progranulin (1)
- Protein complex (1)
- Protein tyrosine modification (1)
- RNA Biology (1)
- RNA turnover (1)
- RNA, long noncoding (1)
- Rapamycin (1)
- Rcf1 (1)
- Redox modification (1)
- Redoxin (1)
- Release of mtDNA and mtRNA (1)
- Respiratory chain (1)
- Reverse electron transfer (1)
- SDH (1)
- SPG8 (1)
- Senescence (1)
- Starvation (1)
- Stem cell (1)
- Stroke (1)
- Stroke genetics (1)
- Subventricular zone (1)
- Superoxide (1)
- TRIM25 (1)
- TWINKLE (1)
- TWNK (1)
- Tissue-specificity (1)
- Transcription factor (1)
- Treatment (1)
- Ubiquitin (1)
- Ubiquitin ligase (1)
- Vitamin (1)
- WASH complex subunit 5 (1)
- adaptive cardiac remodelling (1)
- alternative oxidase (1)
- alternative splicing (1)
- angiogenesis (1)
- aortic aneurysm (1)
- assembly (1)
- ataxia (1)
- atherosclerosis (1)
- cGAS-STING (1)
- cancer metastases (1)
- cardiac ischaemia‐reperfusion (1)
- cardiolipin (1)
- cardiovascular disease (1)
- caspase-2 (1)
- chemotherapy resistance (1)
- colon carcinoma cells (1)
- complex I (1)
- complex I deficiency (1)
- crista junction (1)
- cristae (1)
- cytochrome c oxidase (complex IV) (1)
- data repositories (1)
- diabetes mellitus (1)
- electron transport chain (1)
- epigenomics (1)
- gene expression (1)
- glioblastoma (1)
- hypertension, pulmonary (1)
- i-AAA protease (1)
- intrinsic apoptosis (1)
- ischemia (1)
- leukodystrophy (1)
- long non-coding RNAs (1)
- macrophage (1)
- mass spectrometry (1)
- matrix metalloproteinase (1)
- membrane protein complex (1)
- membrane structure (1)
- metabolomics (1)
- molecular diagnosis (1)
- mouse (1)
- neovascularization, physiologic (1)
- nonsense-mediated mRNA decay (1)
- polyunsaturated fatty acid (1)
- proliferation (1)
- protein complexes (1)
- protein quality control (1)
- protein–protein interaction (1)
- proteomics (1)
- reactive oxygen species (1)
- remodeling (1)
- smooth muscle cell (1)
- strumpellin (1)
- temperature (1)
- therapeutics (1)
- tight junctions (1)
- vascular disease (1)
- vascular integrity (1)
- vascular remodeling (1)
- yeast (1)
Institute
Unmasking a temperature-dependent effect of the P. anserina i-AAA protease on aging and development
(2011)
Different molecular pathways involved in maintaining mitochondrial function are of fundamental importance to control cellular homeostasis. Mitochondrial i-AAA protease is part of such a surveillance system, and PaIAP is the putative ortholog in the fungal aging model Podospora anserina. Here, we investigate the role of PaIAP in aging and development. Deletion of the gene encoding PaIAP resulted in a specific phenotype. When incubated at 27°C, spore germination and fruiting body formation are not different from that of the corresponding wild-type strain. Unexpectedly, the lifespan of the deletion strain is strongly increased. In contrast, cultivation at an elevated temperature of 37°C leads to impairments in spore germination and fruiting body formation and to a reduced lifespan. The higher PaIAP abundance in wild-type strains of the fungus grown at elevated temperature and the phenotype of the deletion strain unmasks a temperature-related role of the protein. The protease appears to be part of a molecular system that has evolved to allow survival under changing temperatures, as they characteristically occur in nature.
Protein turnover and quality control by the proteasome is of paramount importance for cell homeostasis. Dysfunction of the proteasome is associated with aging processes and human diseases such as neurodegeneration, cardiomyopathy, and cancer. The regulation, i.e. activation and inhibition of this fundamentally important protein degradation system, is still widely unexplored. We demonstrate here that the evolutionarily highly conserved type II triple-A ATPase VCP and the proteasome inhibitor PSMF1/PI31 interact directly, and antagonistically regulate proteasomal activity. Our data provide novel insights into the regulation of proteasomal activity.