ArticleMolecular and cellular biology2001
Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 171 citations in OpenAlex.
- A single-amino-acid cleavage controls global mitochondrial complex integrity.Nature structural & molecular biology · 2026Article
- Orchestrating mitochondrial protein import: The emerging role of DYRK1A in health and disease.Protein science : a publication of the Protein Society · 2026Review
- A dynamic gateway: Uncovering the expanded human TOM complex interactome and its regulatory complexity.Science advances · 2026Article
- Proximity Labeling Reveals RNA-Binding Proteins Associating with the Human Mitochondrial Import Receptor TOMM20.Journal of proteome research · 2026Article
- An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import.Structure (London, England : 1993) · 2026Article
- The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import.Advances in experimental medicine and biology · 2026Review
- Structure of the intact Tom20 receptor in the human translocase of the outer membrane complex.PNAS nexus · 2024Article
- DYRK1A signalling synchronizes the mitochondrial import pathways for metabolic rewiring.Nature communications · 2024Article
- Identification of MIMAS, a multifunctional mega-assembly integrating metabolic and respiratory biogenesis factors of mitochondria.Cell reports · 2024Article
- The Adhesion GPCR VLGR1/ADGRV1 Regulates the CaCells · 2022Article
- Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- Dual role of Mic10 in mitochondrial cristae organization and ATP synthase-linked metabolic adaptation and respiratory growth.Cell reports · 2022Article
- Global kinome profiling reveals DYRK1A as critical activator of the human mitochondrial import machinery.Nature communications · 2021Article
- The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation.Molecules (Basel, Switzerland) · 2021Review
- Stress granules inhibit fatty acid oxidation by modulating mitochondrial permeability.Cell reports · 2021Article
- Atomic structure of human TOM core complex.Cell discovery · 2020Article
- Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.Nature structural & molecular biology · 2019Article
- The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells.Scientific reports · 2019Article
- Signaling and Regulation of the Mitochondrial Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2019Review
11 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The preprotein translocase of the yeast mitochondrial outer membrane (TOM) consists of the initial import receptors Tom70 and Tom20 and a approximately 400-kDa (400 K) general import pore (GIP) complex that includes the central receptor Tom22, the channel Tom40, and the three small Tom proteins Tom7, Tom6, and Tom5. We report that the GIP complex is a highly stable complex with an unusual resistance to urea and alkaline pH. Under mild conditions for mitochondrial lysis, the receptor Tom20, but not Tom70, is quantitatively associated with the GIP complex, forming a 500K to 600K TOM complex. A preprotein, stably arrested in the GIP complex, is released by urea but not high salt, indicating that ionic interactions are not essential for keeping the preprotein in the GIP complex. Under more stringent detergent conditions, however, Tom20 and all three small Tom proteins are released, while the preprotein remains in the GIP complex. Moreover, purified outer membrane vesicles devoid of translocase components of the intermembrane space and inner membrane efficiently accumulate the preprotein in the GIP complex. Together, Tom40 and Tom22 thus represent the functional core unit that stably holds accumulated preproteins. The GIP complex isolated from outer membranes exhibits characteristic TOM channel activity with two coupled conductance states, each corresponding to the activity of purified Tom40, suggesting that the complex contains two simultaneously active and coupled channel pores.
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