ArticleMolecular biology of the cell2017
The novel mitochondrial matrix protease Ste23 is required for efficient presequence degradation and processing.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- It Takes Two to Tango: Current Understanding of the Role of M16 Family of Proteases and Their Structural Properties.Biomolecules · 2025Review
- Privileged proteins with a second residence: dual targeting and conditional re-routing of mitochondrial proteins.The FEBS journal · 2024Review
- PPAR-gamma agonist pioglitazone recovers mitochondrial quality control in fibroblasts fromFrontiers in pharmacology · 2023Article
- The Evolutionary History of Peptidases Involved in the Processing of Organelle-Targeting Peptides.Genome biology and evolution · 2022Article
- Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones.RSC advances · 2021Review
- Role of PITRM1 in Mitochondrial Dysfunction and Neurodegeneration.Biomedicines · 2021Review
- Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways.International journal of molecular sciences · 2020Review
- Mitochondrial Proteolysis and Metabolic Control.Cold Spring Harbor perspectives in biology · 2019Review
- Proteomic Characterization of Armillaria mellea Reveals Oxidative Stress Response Mechanisms and Altered Secondary Metabolism Profiles.Microorganisms · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Approximately 70% of mitochondrial precursor proteins are imported from the cytosol via N-terminal presequences, which are cleaved upon exposure to the mitochondrial processing protease MPP in the matrix. Cleaved presequence peptides then need to be efficiently degraded, and impairment of this clearance step, for example, by amyloid β peptides, causes feedback inhibition of MPP, leading ultimately to accumulation of immature precursor proteins within mitochondria. Degradation of mitochondrial peptides is performed by Cym1 in yeast and its homologue, PreP, in humans. Here we identify the novel mitochondrial matrix protease Ste23 in yeast, a homologue of human insulin-degrading enzyme, which is required for efficient peptide degradation. Ste23 and Cym1 tightly cooperate to ensure the correct functioning of the essential presequence processing machinery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.