ArticleMolecular and cellular biology2010
Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 120 citations in OpenAlex.
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- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026Review
- Dysfunctional mitochondria trap proteins in the intermembrane space.The EMBO journal · 2025Article
- The Silencing of theInternational journal of molecular sciences · 2025Article
- Review
- Mitochondrial-derived compartments remove surplus proteins from the outer mitochondrial membrane.The Journal of cell biology · 2024Article
- Identification of factors limiting the allotopic production of the Cox2 subunit of yeast cytochrome c oxidase.Genetics · 2024Article
- New insights into the structure and dynamics of the TOM complex in mitochondria.Biochemical Society transactions · 2024Review
- The MitoLuc assay for the analysis of the mechanism of mitochondrial protein import.Methods in enzymology · 2024Article
- Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- MICU1 controls spatial membrane potential gradients and guides CaCommunications biology · 2022Article
- Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.eLife · 2022Article
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.Cell metabolism · 2021Article
- Mitochondrial compartmentalization: emerging themes in structure and function.Trends in biochemical sciences · 2021Review
- Mapping protein interactions in the active TOM-TIM23 supercomplex.Nature communications · 2021Article
- Mitochondrial Protein Import Dysfunction in Pathogenesis of Neurodegenerative Diseases.Molecular neurobiology · 2021Review
- Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021Review
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial import of cleavable preproteins occurs at translocation contact sites, where the translocase of the outer membrane (TOM) associates with the presequence translocase of the inner membrane (TIM23) in a supercomplex. Different views exist on the mechanism of how TIM23 mediates preprotein sorting to either the matrix or inner membrane. On the one hand, two TIM23 forms were proposed, a matrix transport form containing the presequence translocase-associated motor (PAM; TIM23-PAM) and a sorting form containing Tim21 (TIM23(SORT)). On the other hand, it was reported that TIM23 and PAM are permanently associated in a single-entity translocase. We have accumulated distinct transport intermediates of preproteins to analyze the translocases in their active, preprotein-carrying state. We identified two different forms of active TOM-TIM23 supercomplexes, TOM-TIM23(SORT) and TOM-TIM23-PAM. These two supercomplexes do not represent separate pathways but are in dynamic exchange during preprotein translocation and sorting. Depending on the signals of the preproteins, switches between the different forms of supercomplex and TIM23 are required for the completion of preprotein import.
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