ArticleMolecular biology of the cell2008
Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 76 citations in OpenAlex.
- Tuning the Hsp70 chaperone cycle: emerging roles of GrpE-like nucleotide exchange factors in proteostasis and organelle function.Protein & cell · 2026Review
- Lon/Pim1-mediated degradation of presequence translocase-associated motor components Pam16 and Pam18 in Saccharomyces cerevisiae.The Biochemical journal · 2025Article
- Review
- Article
- A quantitative fluorescence-based approach to study mitochondrial protein import.EMBO reports · 2023Article
- Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021Review
- Article
- Article
- Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44.The Journal of biological chemistry · 2017Article
- Two distinct membrane potential-dependent steps drive mitochondrial matrix protein translocation.The Journal of cell biology · 2017Article
- The non-canonical mitochondrial inner membrane presequence translocase of trypanosomatids contains two essential rhomboid-like proteins.Nature communications · 2016Article
- Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1.Molecular biology of the cell · 2016Article
- The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.3 Biotech · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motor.The Journal of biological chemistry · 2014Article
- The mitochondrial ADP/ATP carrier associates with the inner membrane presequence translocase in a stoichiometric manner.The Journal of biological chemistry · 2014Article
- A complex of Cox4 and mitochondrial Hsp70 plays an important role in the assembly of the cytochrome c oxidase.Molecular biology of the cell · 2013Article
- Generation and analysis of the expressed sequence tags from the mycelium of Ganoderma lucidum.PloS one · 2013Article
- Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012Review
- Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes.The Journal of cell biology · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presequence translocase of the mitochondrial inner membrane (TIM23 complex) mediates the import of preproteins with amino-terminal presequences. To drive matrix translocation the TIM23 complex recruits the presequence translocase-associated motor (PAM) with the matrix heat shock protein 70 (mtHsp70) as central subunit. Activity and localization of mtHsp70 are regulated by four membrane-associated cochaperones: the adaptor protein Tim44, the stimulatory J-complex Pam18/Pam16, and Pam17. It has been proposed that Tim44 serves as molecular platform to localize mtHsp70 and the J-complex at the TIM23 complex, but it is unknown how Pam17 interacts with the translocase. We generated conditional tim44 yeast mutants and selected a mutant allele, which differentially affects the association of PAM modules with TIM23. In tim44-804 mitochondria, the interaction of the J-complex with the TIM23 complex is impaired, whereas unexpectedly the binding of Pam17 is increased. Pam17 interacts with the channel protein Tim23, revealing a new interaction site between TIM23 and PAM. Thus, the motor PAM is composed of functional modules that bind to different sites of the translocase. We suggest that Tim44 is not simply a scaffold for binding of motor subunits but plays a differential role in the recruitment of PAM modules to the inner membrane translocase.
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