ArticleeLife2015
Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026Review
- tRNA Modifications and Dysregulation: Implications for Brain Diseases.Brain sciences · 2024Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- In Vivo Cross-Linking and Co-Immunoprecipitation Procedure to Analyze Nuclear tRNA Export Complexes in Yeast Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A Simple Method for the Detection of Wybutosine-Modified tRNAMethods in molecular biology (Clifton, N.J.) · 2023Article
- Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022Review
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- A novel assay provides insight into tRNAPhe retrograde nuclear import and re-export in S. cerevisiae.Nucleic acids research · 2020Article
- Article
- Oxidative Stress Triggers Selective tRNA Retrograde Transport in Human Cells during the Integrated Stress Response.Cell reports · 2019Article
- tRNA Processing and Subcellular Trafficking Proteins Multitask in Pathways for Other RNAs.Frontiers in genetics · 2019Review
- tRNA dynamics between the nucleus, cytoplasm and mitochondrial surface: Location, location, location.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export.Genes & development · 2017Article
- Multiple Layers of Stress-Induced Regulation in tRNA Biology.Life (Basel, Switzerland) · 2016Review
- Genome-wide screen uncovers novel pathways for tRNA processing and nuclear-cytoplasmic dynamics.Genes & development · 2015Article
- Nucleocytoplasmic shuttling of tRNAs and implication of the cytosolic Hsp70 system in tRNA import.Nucleus (Austin, Tex.) · 2015Article
Corrections and comments
- Commented on by
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
tRNAs are unique among various RNAs in that they shuttle between the nucleus and the cytoplasm, and their localization is regulated by nutrient conditions. Although nuclear export of tRNAs has been well documented, the import machinery is poorly understood. Here, we identified Ssa2p, a major cytoplasmic Hsp70 in Saccharomyces cerevisiae, as a tRNA-binding protein whose deletion compromises nuclear accumulation of tRNAs upon nutrient starvation. Ssa2p recognizes several structural features of tRNAs through its nucleotide-binding domain, but prefers loosely-folded tRNAs, suggesting that Ssa2p has a chaperone-like activity for RNAs. Ssa2p also binds Nup116, one of the yeast nucleoporins. Sis1p and Ydj1p, cytoplasmic co-chaperones for Ssa proteins, were also found to contribute to the tRNA import. These results unveil a novel function of the Ssa2p system as a tRNA carrier for nuclear import by a novel mode of substrate recognition. Such Ssa2p-mediated tRNA import likely contributes to quality control of cytosolic tRNAs.
Indexed as
Identifiers
What OpenQuestion holds
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.