ArticleFEBS letters2016
TIM29 is a subunit of the human carrier translocase required for protein transport.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 71 citations in OpenAlex.
- Sprint interval exercise disrupts mitochondrial ultrastructure driving a unique mitochondrial stress response and remodelling in men.Nature communications · 2025Trial
- Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import.Nature structural & molecular biology · 2026Article
- Genomic and Morphological Insights Into the Adaptive Evolution of Honeybees in Rocky Desertification Habitats.Ecology and evolution · 2026Article
- From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Analysis of the Functional Role of TIMM29 in the Hepatitis B Virus Life Cycle.Microbiology and immunology · 2025Article
- Sengers syndrome caused by biallelic TIMM29 variants and RNAi silencing in Drosophila orthologue recapitulates the human phenotype.Human genomics · 2025Review
- Article
- A High-Throughput Search for SFXN1 Physical Partners Led to the Identification of ATAD3, HSD10 and TIM50.Biology · 2022Article
- Ablation of mitochondrial DNA results in widespread remodeling of the mitochondrial complexome.The EMBO journal · 2021Article
- The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation.Molecules (Basel, Switzerland) · 2021Review
- Review
- Interplay between Mitochondrial Protein Import and Respiratory Complexes Assembly in Neuronal Health and Degeneration.Life (Basel, Switzerland) · 2021Review
- The mitochondrial carrier SFXN1 is critical for complex III integrity and cellular metabolism.Cell reports · 2021Article
- The TIM22 complex mediates the import of sideroflexins and is required for efficient mitochondrial one-carbon metabolism.Molecular biology of the cell · 2021Article
- TIM29 is required for enhanced stem cell activity during regeneration in the flatworm Macrostomum lignano.Scientific reports · 2021Article
- Novel IM-associated protein Tim54 plays a role in the mitochondrial import of internal signal-containing proteins in Trypanosoma brucei.Biology of the cell · 2021Article
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- MICOS assembly controls mitochondrial inner membrane remodeling and crista junction redistribution to mediate cristae formation.The EMBO journal · 2020Article
- Biogenesis of Mitochondrial Metabolite Carriers.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrophobic inner mitochondrial membrane proteins with internal targeting signals, such as the metabolite carriers, use the carrier translocase (TIM22 complex) for transport into the inner membrane. Defects in this transport pathway have been associated with neurodegenerative disorders. While the TIM22 complex is well studied in baker's yeast, very little is known about the mammalian TIM22 complex. Using immunoprecipitation, we purified the human carrier translocase and identified a mitochondrial inner membrane protein TIM29 as a novel component, specific to metazoa. We show that TIM29 is a constituent of the 440 kDa TIM22 complex and interacts with oxidized TIM22. Our analyses demonstrate that TIM29 is required for the structural integrity of the TIM22 complex and for import of substrate proteins by the carrier translocase.
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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.