ArticleJournal of molecular biology2017
Identification of a Degradation Signal Sequence within Substrates of the Mitochondrial i-AAA Protease.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- Recognition of small Tim chaperones by the mitochondrial Yme1 protease.Protein science : a publication of the Protein Society · 2026Article
- The role of mitochondrial proteases in inflammation and immunity.Frontiers in immunology · 2026Review
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants.Biochemical Society transactions · 2022Review
- Review
- Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.eLife · 2020Article
- Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019Review
- Mitochondrial AAA proteases: A stairway to degradation.Mitochondrion · 2019Review
- Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.Molecular cell · 2019Article
- Autophagy accounts for approximately one-third of mitochondrial protein turnover and is protein selective.Autophagy · 2019Article
- Mitochondrial Proteolysis and Metabolic Control.Cold Spring Harbor perspectives in biology · 2019Review
- Review
- Dissecting Substrate Specificities of the Mitochondrial AFG3L2 Protease.Biochemistry · 2018Article
- Molecular insights into theThe Journal of biological chemistry · 2017Article
- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Science (New York, N.Y.) · 2017Article
- Metalloproteases of the Inner Mitochondrial Membrane.Biochemistry · 2017Review
- Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The i-AAA protease is a component of the mitochondrial quality control machinery that regulates respiration, mitochondrial dynamics, and protein import. The protease is required to select specific substrates for degradation from among the diverse complement of proteins present in mitochondria, yet the rules that govern this selection are unclear. Here, we reconstruct the yeast i-AAA protease, Yme1p, to examine the in vitro degradation of two intermembrane space chaperone subunits, Tim9 and Tim10. Yme1p degrades Tim10 more rapidly than Tim9 despite high sequence and structural similarity, and loss of Tim10 is accelerated by the disruption of conserved disulfide bonds within the substrate. An unstructured N-terminal region of Tim10 is necessary and sufficient to target the substrate to the protease through recognition of a short phenylalanine-rich motif, and the presence of similar motifs in other small Tim proteins predicts robust degradation by the protease. Together, these results identify the first specific degron sequence within a native i-AAA protease substrate.
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Registered trials
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