ArticleThe EMBO journal1996
Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 183 citations in OpenAlex.
- Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Deeply conserved and expressed small ORFs in the model beetle Tribolium castaneum.BMC biology · 2026Article
- A dynamic gateway: Uncovering the expanded human TOM complex interactome and its regulatory complexity.Science advances · 2026Article
- Autophagy activation by the Becn1Brain, behavior, and immunity · 2026Article
- The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import.Advances in experimental medicine and biology · 2026Review
- Renovascular Disease and Mitochondrial Dysfunction in Human Mesenchymal Stem Cells.Journal of the American Society of Nephrology : JASN · 2024Article
- Autosomal recessive progeroid syndrome due to homozygosity for a TOMM7 variant.The Journal of clinical investigation · 2022Article
- Host genetic diversity and genetic variations of SARS-CoV-2 in COVID-19 pathogenesis and the effectiveness of vaccination.International immunopharmacology · 2022Review
- Article
- Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.Journal of molecular biology · 2021Review
- Review
- Genetic variants are identified to increase risk of COVID-19 related mortality from UK Biobank data.Human genomics · 2021Article
- Genetic variants are identified to increase risk of COVID-19 related mortality from UK Biobank data.medRxiv : the preprint server for health sciences · 2020Article
- Msp1 cooperates with the proteasome for extraction of arrested mitochondrial import intermediates.Molecular biology of the cell · 2020Article
- Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.Nature structural & molecular biology · 2019Article
- Does aberrant membrane transport contribute to poor outcome in adult acute myeloid leukemia?Frontiers in pharmacology · 2015Article
- A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria.PLoS biology · 2014Article
- Viral product trafficking to mitochondria, mechanisms and roles in pathogenesis.Infectious disorders drug targets · 2012Review
- Localization of mRNAs coding for mitochondrial proteins in the yeast Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2011Article
- Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The preprotein translocase of the outer mitochondrial membrane is a multi-subunit complex with receptors and a general import pore. We report the molecular identification of Tom7, a small subunit of the translocase that behaves as an integral membrane protein. The deletion of TOM7 inhibited the mitochondrial import of the outer membrane protein porin, whereas the import of preproteins destined for the mitochondrial interior was impaired only slightly. However, protein import into the mitochondrial interior was strongly inhibited when it occurred in two steps: preprotein accumulation at the outer membrane in the absence of a membrane potential and subsequent further import after the re-establishment of a membrane potential. The delay of protein import into tom7delta mitochondria seemed to occur after the binding of preproteins to the outer membrane receptor sites. A lack of Tom7 stabilized the interaction between the receptors Tom20 and Tom22 and the import pore component Tom40. This indicated that Tom7 exerts a destabilizing effect on part of the outer membrane translocase, whereas Tom6 stabilizes the interaction between the receptors and the import pore. Synthetic growth defects of the double mutants tom7delta tom20delta and tom7delta tom6delta provided genetic evidence for the functional relationship of Tom7 with Tom20 and Tom6. These results suggest that (i) Tom7 plays a role in sorting and accumulation of the preproteins at the outer membrane, and (ii) Tom7 and Tom6 perform complementary functions in modulating the dynamics of the outer membrane translocase.
Indexed as
Identifiers
8641278PMC450135W40646405What OpenQuestion 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 OpenQuestion graph.