ArticleThe Journal of cell biology1996
In vivo nuclear transport kinetics in Saccharomyces cerevisiae: a role for heat shock protein 70 during targeting and translocation.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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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
88 citing papers in PubMed, 205 citations in OpenAlex.
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Article
- Review
- Exportin Crm1 is important for Swi6 nuclear shuttling and MBF transcription activation in Saccharomyces cerevisiae.BMC molecular and cell biology · 2022Article
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease-The Example of C9orf72 ALS.International journal of molecular sciences · 2021Review
- NaScience advances · 2021Article
- Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.Molecular and cellular biology · 2020Article
- Article
- Age-dependent deterioration of nuclear pore assembly in mitotic cells decreases transport dynamics.eLife · 2019Article
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing.The EMBO journal · 2016Article
- Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae.The Journal of cell biology · 2015Article
- Neurospora importin α is required for normal heterochromatic formation and DNA methylation.PLoS genetics · 2015Article
- Yeast importin-α (Srp1) performs distinct roles in the import of nuclear proteins and in targeting proteasomes to the nucleus.The Journal of biological chemistry · 2014Article
- Genome-wide identification of heat shock proteins (Hsps) and Hsp interactors in rice: Hsp70s as a case study.BMC genomics · 2014Article
- Esophageal cancer alters the expression of nuclear pore complex binding protein Hsc70 and eIF5A-1.Functional & integrative genomics · 2013Article
- A subset of FG-nucleoporins is necessary for efficient Msn5-mediated nuclear protein export.Biochimica et biophysica acta · 2013Article
- 70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY.The Journal of biological chemistry · 2013Article
- Tunable signal processing through modular control of transcription factor translocation.Science (New York, N.Y.) · 2013Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The transport of proteins into the nucleus is a receptor-mediated process that is likely to involve between 50-100 gene products, including many that comprise the nuclear pore complex. We have developed an assay in Saccharomyces cerevisiae for the nuclear transport of green fluorescent protein fused to the SV-40 large T antigen nuclear localization signal (NLS-GFP). This assay allows the measurement of relative NLS-GFP nuclear import rates in wild-type and mutant cells under various physiological conditions. Probably the best understood component of the nuclear transport apparatus is Srp1p, the NLS receptor, which binds NLS-cargo in the cytoplasm and accompanies it into the nucleus. When compared to SRP1+ cells, NLS-GFP import rates in temperature-sensitive srp1-31 cells were slower and showed a lower temperature optimum. The in vivo transport defect of the srp1-31 cells was correlated with the purified protein's thermal sensitivity, as assayed by in vitro NLS peptide binding. We show that the kinetics of NLS-directed nuclear transport in wild-type cells is stimulated by the elevated expression of SSA1, which encodes a cytoplasmic heat shock protein 70 (Hsp70). Elevated Hsp70 levels are sufficient to suppress the NLS-GFP import defects in srp1-31 and nup82-3 cells. NUP82 encodes a protein that functions within the nuclear pore complex subsequent to docking. These results provide genetic evidence that Hsp70 acts during both targeting and translocation phases of nuclear transport, possibly as a molecular chaperone to promote the formation and stability of the Srp1p-NLS-cargo complex.
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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.