ArticleThe Journal of cell biology2017
Two distinct membrane potential-dependent steps drive mitochondrial matrix protein translocation.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Ubiquitination-mediated degradation of NLRX1 drives metabolic vulnerability and accelerates intervertebral disc degeneration.Cell death and differentiation · 2026Article
- Mitochondrial presequences harbor variable strengths to maintain organellar function.The Journal of cell biology · 2026Article
- TbTim20 facilitates protein import at a low membrane potential in trypanosomes lacking the mitochondrial genome.The FEBS journal · 2026Article
- Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Protein insertion into the inner membrane of mitochondria: routes and mechanisms.FEBS open bio · 2024Review
- A hybrid TIM complex mediates protein import into hydrogenosomes of Trichomonas vaginalis.BMC biology · 2024Article
- OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.The Journal of cell biology · 2024Article
- Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease.Molecular and cellular biology · 2024Article
- Mitochondrial Quality Control via Mitochondrial Unfolded Protein Response (mtUPR) in Ageing and Neurodegenerative Diseases.Biomolecules · 2023Review
- Protein import into mitochondria - a new path through the membranes.Nature structural & molecular biology · 2023Article
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.eLife · 2022Article
- Prescription drugs and mitochondrial metabolism.Bioscience reports · 2022Review
- DELE1 tracks perturbed protein import and processing in human mitochondria.Nature communications · 2022Article
- Global mitochondrial protein import proteomics reveal distinct regulation by translation and translocation machinery.Molecular cell · 2022Article
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
- Dissecting the molecular mechanisms of mitochondrial import and maturation of peroxiredoxins from yeast and mammalian cells.Biophysical reviews · 2021Review
- From OCR and ECAR to energy: Perspectives on the design and interpretation of bioenergetics studies.The Journal of biological chemistry · 2021Review
- Mapping protein interactions in the active TOM-TIM23 supercomplex.Nature communications · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two driving forces energize precursor translocation across the inner mitochondrial membrane. Although the membrane potential (Δψ) is considered to drive translocation of positively charged presequences through the TIM23 complex (presequence translocase), the activity of the Hsp70-powered import motor is crucial for the translocation of the mature protein portion into the matrix. In this study, we show that mitochondrial matrix proteins display surprisingly different dependencies on the Δψ. However, a precursor's hypersensitivity to a reduction of the Δψ is not linked to the respective presequence, but rather to the mature portion of the polypeptide chain. The presequence translocase constituent Pam17 is specifically recruited by the receptor Tim50 to promote the transport of hypersensitive precursors into the matrix. Our analyses show that two distinct Δψ-driven translocation steps energize precursor passage across the inner mitochondrial membrane. The Δψ- and Pam17-dependent import step identified in this study is positioned between the two known energy-dependent steps: Δψ-driven presequence translocation and adenosine triphosphate-driven import motor activity.
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