ArticleThe Journal of cell biology2001
The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 141 citations in OpenAlex.
- A systematic interactome ofeLife · 2026Article
- Targeting colorectal cancer at the level of nuclear pore complex.Journal of advanced research · 2025Review
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- CRZ1 transcription factor is involved in cell survival, stress tolerance, and virulence in fungi.Journal of biosciences · 2022Review
- Nuclear transport genes recurrently duplicate by means of RNA intermediates in Drosophila but not in other insects.BMC genomics · 2021Article
- Chaperoning RPA during DNA metabolism.Current genetics · 2019Review
- Genetic screen of the yeast environmental stress response dynamics uncovers distinct regulatory phases.Molecular systems biology · 2019Article
- Engineered SUMO/protease system identifies Pdr6 as a bidirectional nuclear transport receptor.The Journal of cell biology · 2019Article
- Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122.The Journal of cell biology · 2019Article
- Fine tuning the level of the Cdc13 telomere-capping protein for maximal chromosome stability performance.Current genetics · 2019Review
- tRNA Processing and Subcellular Trafficking Proteins Multitask in Pathways for Other RNAs.Frontiers in genetics · 2019Review
- Xpo7 is a broad-spectrum exportin and a nuclear import receptor.The Journal of cell biology · 2018Article
- Extensive Identification and In-depth Validation of Importin 13 Cargoes.Molecular & cellular proteomics : MCP · 2018Article
- Nuclear import of Cdc13 limits chromosomal capping.Nucleic acids research · 2018Article
- Casein Kinase I Isoform Hrr25 Is a Negative Regulator of Haa1 in the Weak Acid Stress Response Pathway in Saccharomyces cerevisiae.Applied and environmental microbiology · 2017Article
- Nuclear import of dimerized ribosomal protein Rps3 in complex with its chaperone Yar1.Scientific reports · 2016Article
- Structural and functional characterization of ybr137wp implicates its involvement in the targeting of tail-anchored proteins to membranes.Molecular and cellular biology · 2014Article
- Characterization of karyopherins in androgen receptor intracellular trafficking in the yeast model.International journal of clinical and experimental pathology · 2014Article
- Structural basis for the nuclear export activity of Importin13.The EMBO journal · 2013Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified a novel pathway for protein import into the nucleus. Although the product of Saccharomyces cerevisiae gene MSN5 was previously shown to function as a karyopherin (Kap) for nuclear export of various proteins, we discovered a nuclear import pathway mediated by Msn5p (also referred to as Kap142p). We have purified from yeast cytosol a complex containing Kap142p and the trimeric replication protein A (RPA), which is required for multiple aspects of DNA metabolism, including DNA replication, DNA repair, and recombination. In wild-type cells, RPA was localized primarily to the nucleus but, in a KAP142 deletion strain, RPA was mislocalized to the cytoplasm and the strain was highly sensitive to bleomycin (BLM). BLM causes DNA double-strand breaks and, in S. cerevisiae, the DNA damage is repaired predominantly by RPA-dependent homologous recombination. Therefore, our results indicate that in wild-type cells a critical portion of RPA was imported into the nucleus by Kap142p. Like several other import-related Kap-substrate complexes, the endogenous RPA-Kap142p complex was dissociated by RanGTP, but not by RanGDP. All three RPA genes are essential for viability, whereas KAP142 is not. Perhaps explaining this disparity, we observed an interaction between RPA and Kap95p in a strain lacking Kap142p. This interaction could provide a mechanism for import of RPA into the nucleus and cell viability in the absence of Kap142p. Together with published results (Kaffman, A., N.M. Rank, E.M. O'Neill, L.S. Huang, and E.K. O'Shea. 1998. Nature. 396:482-486; Blondel, M., P.M. Alepuz, L.S. Huang, S. Shaham, G. Ammerer, and M. Peter. 1999. Genes Dev. 13:2284-2300; DeVit, M.J., and M. Johnston. 1999. Curr. Biol. 9:1231-1241; Mahanty, S.K., Y. Wang, F.W. Farley, and E.A. Elion. 1999. Cell. 98:501-512) our data indicate that the karyopherin Kap142p is able to mediate nuclear import of one set of proteins and nuclear export of a different set of proteins.
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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.