ArticleNature structural & molecular biology2025
Dynamic TOM-TIM23 supercomplex directs mitochondrial protein translocation and sorting.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Topogenic sequence recognition at TIM complexes revealed by a stendomycin-bound structure.Nature chemical biology · 2026Article
- Fructose directly remodels the translocase of the outer membrane to impair oxidative phosphorylation in podocytes.Signal transduction and targeted therapy · 2026Article
- Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import.Nature structural & molecular biology · 2026Article
- A coupled TOM-TIM22 supercomplex in human mitochondrial protein import.Nature structural & molecular biology · 2026Article
- YlmG1 is localized exclusively to the chloroplast envelope membrane and is involved in preprotein translocation in Arabidopsis thaliana.FEBS open bio · 2026Article
- Transmembrane domain switching controls PINK1 import and fate in mitochondria.The EMBO journal · 2026Article
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- Lamin A/C as a biomarker for breast cancer.Molecular biology reports · 2025Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial translocase of the outer membrane (TOM) and translocase of the inner membrane 23 (TIM23) complexes are coupled to control protein import across the outer and inner membranes, respectively. However, the mechanisms of protein recognition and sorting in the TOM-TIM23 pathway remain unclear. Here we report cryo-electron microscopy structures of a translocating polypeptide substrate captured in the active TOM-TIM23 supercomplex from Saccharomyces cerevisiae. In the TOM complex, the polypeptide substrate adopts multiple conformations stabilized by hydrophilic residues from distinct regions of the Tom40 channel. In the TIM23 complex, the Tim17 and Mgr2 subunits create the translocation pathway, with a central restriction formed by four highly conserved hydrophobic residues. The substrate primarily interacts with hydrophobic residues along the Tim17-Mgr2 pathway. Substrate hydrophobicity modulates the association of Mgr2 with Tim17, enabling dynamic regulation of protein sorting toward either the matrix or membrane. These findings reveal a sophisticated translocation mechanism of the TOM-TIM23 supercomplex that ensures the efficient import of diverse mitochondrial proteins.
Indexed as
Identifiers
40877479What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.