ArticleThe EMBO journal2003
Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- Topogenic sequence recognition at TIM complexes revealed by a stendomycin-bound structure.Nature chemical biology · 2026Article
- A coupled TOM-TIM22 supercomplex in human mitochondrial protein import.Nature structural & molecular biology · 2026Article
- Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import.Nature structural & molecular biology · 2026Article
- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Identification of a novel MIPEP splice variant with altered substrate-binding properties.Biochemistry and biophysics reports · 2025Article
- Dynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex.Journal of chemical information and modeling · 2025Article
- OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.The Journal of cell biology · 2024Article
- The architecture of substrate-engaged TOM-TIM23 supercomplex reveals preprotein proximity sites for mitochondrial protein translocation.Cell discovery · 2024Article
- Rescue of mitochondrial import failure by intercellular organellar transfer.Nature communications · 2024Article
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- Molecular pathway of mitochondrial preprotein import through the TOM-TIM23 supercomplex.Nature structural & molecular biology · 2023Article
- Article
- A two-step mitochondrial import pathway couples the disulfide relay with matrix complex I biogenesis.The Journal of cell biology · 2023Article
- Aggregation-prone Tau impairs mitochondrial import, which affects organelle morphology and neuronal complexity.Journal of cell science · 2023Article
- The UbiB family member Cqd1 forms a novel membrane contact site in mitochondria.Journal of cell science · 2023Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- 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
- The Role of Mitochondrial Quality Control in Anthracycline-Induced Cardiotoxicity: From Bench to Bedside.Oxidative medicine and cellular longevity · 2022Review
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Preproteins with N-terminal presequences are imported into mitochondria at translocation contact sites that include the translocase of the outer membrane (TOM complex) and the presequence translocase of the inner membrane (TIM23 complex). Little is known about the functional cooperation of these translocases. We have characterized translocation contact sites by a productive TOM-TIM-preprotein supercomplex to address the role of three translocase subunits that expose domains to the intermembrane space (IMS). The IMS domain of the receptor Tom22 is required for stabilization of the translocation contact site supercomplex. Surprisingly, the N-terminal segment of the channel Tim23, which tethers the TIM23 complex to the outer membrane, is dispensable for both protein import and generation of the TOM-TIM supercomplex. Tim50, with its large IMS domain, is crucial for generation but not for stabilization of the supercomplex. Thus, Tim50 functions as a dynamic factor and the IMS domain of Tom22 represents a stabilizing element in formation of a productive translocation contact site supercomplex.
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