ArticleeLife2022
Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Translational antagonism enables bet-hedging in yeast via mitochondrial bistability.bioRxiv : the preprint server for biology · 2026Article
- Intercellular mitochondrial transfer and trans-mitophagy in response to protein import dysfunction.The Journal of cell biology · 2026Article
- Mitochondrial Proteostasis Links Diabetes and Sarcopenia: Cross-Scale Convergence from Experimental Models to Human Multi-Omics.Diabetes & metabolism journal · 2026Review
- Proteostasis of organelles in aging and disease.The FEBS journal · 2026Review
- Transmembrane domain switching controls PINK1 import and fate in mitochondria.The EMBO journal · 2026Article
- Mitochondrial presequences harbor variable strengths to maintain organellar function.The Journal of cell biology · 2026Article
- Dynamic TOM-TIM23 supercomplex directs mitochondrial protein translocation and sorting.Nature structural & molecular biology · 2025Article
- Design of diverse, functional mitochondrial targeting sequences across eukaryotic organisms using variational autoencoder.Nature communications · 2025Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Modulation of mitochondrial voltage dependent anion channel: studies on bilayer electrophysiology.Frontiers in physiology · 2025Review
- Article
- New insights into the structure and dynamics of the TOM complex in mitochondria.Biochemical Society transactions · 2024Review
- Rescue of mitochondrial import failure by intercellular organellar transfer.Nature communications · 2024Article
- The MitoLuc assay for the analysis of the mechanism of mitochondrial protein import.Methods in enzymology · 2024Article
- MitoLuc: A Luminescence-Based Assay to Study Real-Time Protein Import into Mitochondria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Co-fractionation-mass spectrometry to characterize native mitochondrial protein assemblies in mammalian neurons and brain.Nature protocols · 2023Article
- ATP yield of plant respiration: potential, actual and unknown.Annals of botany · 2023Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Protein-Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B'ζ Holoenzyme.Plants (Basel, Switzerland) · 2023Article
- The MitoLuc Assay System for Accurate Real-Time Monitoring of Mitochondrial Protein Import Within Mammalian Cells.Journal of molecular biology · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Nearly all mitochondrial proteins need to be targeted for import from the cytosol. For the majority, the first port of call is the translocase of the outer membrane (TOM complex), followed by a procession of alternative molecular machines, conducting transport to their final destination. The pre-sequence translocase of the inner membrane (TIM23-complex) imports proteins with cleavable pre-sequences. Progress in understanding these transport mechanisms has been hampered by the poor sensitivity and time resolution of import assays. However, with the development of an assay based on split NanoLuc luciferase, we can now explore this process in greater detail. Here, we apply this new methodology to understand how ∆ψ and ATP hydrolysis, the two main driving forces for import into the matrix, contribute to the transport of pre-sequence-containing precursors (PCPs) with varying properties. Notably, we found that two major rate-limiting steps define PCP import time: passage of PCP across the outer membrane and initiation of inner membrane transport by the pre-sequence - the rates of which are influenced by PCP size and net charge. The apparent distinction between transport through the two membranes (passage through TOM is substantially complete before PCP-TIM engagement) is in contrast with the current view that import occurs through TOM and TIM in a single continuous step. Our results also indicate that PCPs spend very little time in the TIM23 channel - presumably rapid success or failure of import is critical for maintenance of mitochondrial fitness.
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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 Socratic graph.