ArticleThe Journal of cell biology2011
Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 100 citations in OpenAlex.
- Review
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- A quantitative fluorescence-based approach to study mitochondrial protein import.EMBO reports · 2023Article
- Post-translational modifications and protein quality control of mitochondrial channels and transporters.Frontiers in cell and developmental biology · 2023Review
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Protein import motor complex reacts to mitochondrial misfolding by reducing protein import and activating mitophagy.Nature communications · 2022Article
- Mapping protein interactions in the active TOM-TIM23 supercomplex.Nature communications · 2021Article
- Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones.RSC advances · 2021Review
- Coordinated Translocation of Presequence-Containing Precursor Proteins Across Two Mitochondrial Membranes: Knowns and Unknowns of How TOM and TIM23 Complexes Cooperate With Each Other.Frontiers in physiology · 2021Review
- Long non-coding RNA LOC100133669 promotes cell proliferation in oesophageal squamous cell carcinoma.Cell proliferation · 2020Article
- COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria.Journal of molecular biology · 2020Article
- Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.Nature structural & molecular biology · 2019Article
- A mutagenesis analysis of Tim50, the major receptor of the TIM23 complex, identifies regions that affect its interaction with Tim23.Scientific reports · 2019Article
- ROMO1 is a constituent of the human presequence translocase required for YME1L protease import.The Journal of cell biology · 2019Article
- Inner Mitochondrial Translocase Tim50 Is Central in Adrenal and Testicular Steroid Synthesis.Molecular and cellular biology · 2019Article
- Motor recruitment to the TIM23 channel's lateral gate restricts polypeptide release into the inner membrane.Nature communications · 2018Article
- Mutations inEMBO molecular medicine · 2018Article
- Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.Science advances · 2017Article
- Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.eLife · 2017Article
- Mitochondrial epileptic encephalopathy, 3-methylglutaconic aciduria and variable complex V deficiency associated with TIMM50 mutations.Clinical genetics · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner.
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Registered trials
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