ArticleMolecular and cellular biology2008
The assembly pathway of the mitochondrial carrier translocase involves four preprotein translocases.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 68 citations in OpenAlex.
- Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import.Nature structural & molecular biology · 2026Article
- From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026Review
- Article
- The Journey of Mitochondrial Protein Import and the Roadmap to Follow.International journal of molecular sciences · 2023Review
- The mitochondrial protein Sideroflexin 3 (SFXN3) influences neurodegeneration pathways in vivo.The FEBS journal · 2022Article
- 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
- Role of the Mitochondrial Protein Import Machinery and Protein Processing in Heart Disease.Frontiers in cardiovascular medicine · 2021Review
- Biogenesis of Mitochondrial Metabolite Carriers.Biomolecules · 2020Review
- Defining the Substrate Spectrum of the TIM22 Complex Identifies Pyruvate Carrier Subunits as Unconventional Cargos.Current biology : CB · 2020Article
- The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments.BMC biology · 2020Article
- A trypanosomal orthologue of an intermembrane space chaperone has a non-canonical function in biogenesis of the single mitochondrial inner membrane protein translocase.PLoS pathogens · 2017Article
- Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease.The Biochemical journal · 2017Review
- Granzyme B enters the mitochondria in a Sam50-, Tim22- and mtHsp70-dependent manner to induce apoptosis.Cell death and differentiation · 2017Article
- TIM29 is a subunit of the human carrier translocase required for protein transport.FEBS letters · 2016Article
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- Intramolecular disulfide bond of Tim22 protein maintains integrity of the TIM22 complex in the mitochondrial inner membrane.The Journal of biological chemistry · 2014Article
- Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria.Molecular biology of the cell · 2013Article
- The channel-forming Sym1 protein is transported by the TIM23 complex in a presequence-independent manner.Molecular and cellular biology · 2012Article
- Mitochondrial protein synthesis, import, and assembly.Genetics · 2012Article
- Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012Review
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial inner membrane contains preprotein translocases that mediate insertion of hydrophobic proteins. Little is known about how the individual components of these inner membrane preprotein translocases combine to form multisubunit complexes. We have analyzed the assembly pathway of the three membrane-integral subunits Tim18, Tim22, and Tim54 of the twin-pore carrier translocase. Tim54 displayed the most complex pathway involving four preprotein translocases. The precursor is translocated across the intermembrane space in a supercomplex of outer and inner membrane translocases. The TIM10 complex, which translocates the precursor of Tim22 through the intermembrane space, functions in a new posttranslocational manner: in case of Tim54, it is required for the integration of Tim54 into the carrier translocase. Tim18, the function of which has been unknown so far, stimulates integration of Tim54 into the carrier translocase. We show that the carrier translocase is built via a modular process and that each subunit follows a different assembly route. Membrane insertion and assembly into the oligomeric complex are uncoupled for each precursor protein. We propose that the mitochondrial assembly machinery has adapted to the needs of each membrane-integral subunit and that the uncoupling of translocation and oligomerization is an important principle to ensure continuous import and assembly of protein complexes in a highly active membrane.
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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.