ArticleThe Journal of biological chemistry2010
Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 96 citations in OpenAlex.
- Lon/Pim1-mediated degradation of presequence translocase-associated motor components Pam16 and Pam18 in Saccharomyces cerevisiae.The Biochemical journal · 2025Article
- Lon-dependent proteolysis in oxidative stress responses.Journal of bacteriology · 2025Review
- Vacuolar degradation of plant organelles.The Plant cell · 2024Review
- The Regulation of the Disease-Causing GeneCells · 2024Review
- Newly imported proteins in mitochondria are particularly sensitive to aggregation.Acta physiologica (Oxford, England) · 2023Article
- The mitochondrial Hsp70 controls the assembly of the FNature communications · 2023Article
- Pharmacological Progress of Mitophagy Regulation.Current neuropharmacology · 2023Article
- Posttranslational regulation of mitochondrial frataxin and identification of compounds that increase frataxin levels in Friedreich's ataxia.The Journal of biological chemistry · 2022Article
- Organismal and Cellular Stress Responses upon Disruption of Mitochondrial Lonp1 Protease.Cells · 2022Article
- Review
- Article
- Mrx6 regulates mitochondrial DNA copy number inMolecular biology of the cell · 2020Article
- The Mitochondrial Lon Protease: Novel Functions off the Beaten Track?Biomolecules · 2020Review
- Acute increases inAmerican journal of physiology. Cell physiology · 2019Article
- Review
- LONP1 Is Required for Maturation of a Subset of Mitochondrial Proteins, and Its Loss Elicits an Integrated Stress Response.Molecular and cellular biology · 2018Article
- Mitochondrial Lon sequesters and stabilizes p53 in the matrix to restrain apoptosis under oxidative stress via its chaperone activity.Cell death & disease · 2018Article
- IMiQ: a novel protein quality control compartment protecting mitochondrial functional integrity.Molecular biology of the cell · 2018Article
- Lon protease inactivation inCell death discovery · 2018Article
- The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP-dependent proteases are currently emerging as key regulators of mitochondrial functions. Among these proteolytic systems, Pim1, a Lon-like serine protease in Saccharomyces cerevisiae, is involved in the control of selective protein turnover in the mitochondrial matrix. In the absence of Pim1, yeast cells have been shown to accumulate electron-dense inclusion bodies in the matrix space, to lose integrity of mitochondrial genome, and to be respiration-deficient. Because of the severity of phenotypes associated with the depletion of Pim1, this protease appears to be an essential component of the protein quality control machinery in mitochondria and to exert crucial functions during the biogenesis of this organelle. Nevertheless, its physiological substrates and partners are not fully characterized. Therefore, we used the combination of different proteomic techniques to assess the nature of oxidized protein substrates and physiological partners of Pim1 protease under non-repressing growth conditions. The results presented here supply evidence that Pim1-mediated proteolysis is required for elimination of oxidatively damaged proteins in mitochondria.
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