ArticleGenetics2012
Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.
Article in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Wiring of cellular proteostasis by J-domain proteins.Cell stress & chaperones · 2026Review
- Article
- Article
- Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import.The Journal of biological chemistry · 2021Article
- Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase.International journal of molecular sciences · 2021Review
- ALS/FTD mutations in UBQLN2 are linked to mitochondrial dysfunction through loss-of-function in mitochondrial protein import.Human molecular genetics · 2021Article
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- Insight into the Interactome of Intramitochondrial PKA Using Biotinylation-Proximity Labeling.International journal of molecular sciences · 2020Article
- Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.Open biology · 2020Review
- Motor recruitment to the TIM23 channel's lateral gate restricts polypeptide release into the inner membrane.Nature communications · 2018Article
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Origin and Evolutionary Alteration of the Mitochondrial Import System in Eukaryotic Lineages.Molecular biology and evolution · 2017Article
- Article
- Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.Molecular and cellular biology · 2017Article
- Article
- 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
- Dissecting stop transfer versus conservative sorting pathways for mitochondrial inner membrane proteins in vivo.The Journal of biological chemistry · 2013Article
- Comparative analysis of putative orthologues of mitochondrial import motor subunit: Pam18 and Pam16 in plants.PloS one · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A highly conserved, Hsp70-based, import motor, which is associated with the translocase on the matrix side of the inner mitochondrial membrane, is critical for protein translocation into the matrix. Hsp70 is tethered to the translocon via interaction with Tim44. Pam18, the J-protein co-chaperone, and Pam16, a structurally related protein with which Pam18 forms a heterodimer, are also critical components of the motor. Their N termini are important for the heterodimer's translocon association, with Pam18's and Pam16's N termini interacting in the intermembrane space and the matrix, respectively. Here, using the model organism Saccharomyces cerevisiae, we report the identification of an N-terminal segment of Tim44, important for association of Pam16 with the translocon. We also report that higher amounts of Pam17, a nonessential motor component, are found associated with the translocon in both PAM16 and TIM44 mutants that affect their interaction with one another. These TIM44 and PAM16 mutations are also synthetically lethal with a deletion of PAM17. In contrast, a deletion of PAM17 has little, or no genetic interaction with a PAM18 mutation that affects translocon association of the Pam16:Pam18 heterodimer, suggesting a second role for the Pam16:Tim44 interaction. A similar pattern of genetic interactions and enhanced Pam17 translocon association was observed in the absence of the C terminus of Tim17, a core component of the translocon. We suggest the Pam16:Tim44 interaction may play two roles: (1) tethering the Pam16:Pam18 heterodimer to the translocon and (2) positioning the import motor for efficient engagement with the translocating polypeptide along with Tim17 and Pam17.
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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.