ArticleThe Journal of cell biology1991
A yeast protein that binds nuclear localization signals: purification localization, and antibody inhibition of binding activity.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
- Role of casein kinase 1 in the glucose sensor-mediated signaling pathway in yeast.BMC cell biology · 2010Article
- The small GTPase Gsp1p binds to the repeat domain of the nucleoporin Nsp1p.The Biochemical journal · 1998Article
- Characterization of a Drosophila phosphorylation-dependent nuclear-localization-signal-binding protein.The Biochemical journal · 1997Article
- Nucleocytoplasmic transport of macromolecules.Microbiology and molecular biology reviews : MMBR · 1997Review
- Mutants in a yeast Ran binding protein are defective in nuclear transport.The EMBO journal · 1995Article
- The regulation of protein transport to the nucleus by phosphorylation.The Biochemical journal · 1995Review
- The yeast nuclear import receptor is required for mitosis.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Isolation of a yeast protein kinase that is activated by the protein encoded by SRP1 (Srp1p) and phosphorylates Srp1p complexed with nuclear localization signal peptides.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- The serum response factor nuclear localization signal: general implications for cyclic AMP-dependent protein kinase activity in control of nuclear translocation.Molecular and cellular biology · 1995Article
- Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope.The Journal of cell biology · 1994Article
- Reconstitution of nuclear protein transport with semi-intact yeast cells.The Journal of cell biology · 1993Article
- Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae.Genetics · 1993Article
- A cytoplasmically anchored nuclear protein interferes specifically with the import of nuclear proteins but not U1 snRNA.The Journal of cell biology · 1993Article
- The complete general secretory pathway in gram-negative bacteria.Microbiological reviews · 1993Review
- Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins.The Journal of cell biology · 1992Article
- Analysis of a developmentally regulated nuclear localization signal in Xenopus.The Journal of cell biology · 1992Article
- Nuclear transport and nuclear pores in yeast.Antonie van Leeuwenhoek · 1992Review
- A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast.Molecular biology of the cell · 1992Article
- A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import.The Journal of cell biology · 1992Article
- Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways.The Journal of cell biology · 1992Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Short stretches of amino acids, termed nuclear localization sequences (NLS), can mediate assembly of proteins into the nucleus. Proteins from the yeast, Saccharomyces cerevisiae, have been identified that specifically recognize nuclear localization peptides (Silver, P., I. Sadler, and M. A. Osborne. 1989. J. Cell Biol. 109:983-989). We now further define the role of one of these NLS-binding proteins in nuclear protein localization. The NLS-binding protein of 70-kD molecular mass can be purified from salt extracts of nuclei. Antibodies raised against the NLS-binding protein localized the protein mainly to the nucleus with minor amounts in the cytoplasm. These antibodies also inhibited the association of NLS-protein conjugates with nuclei. Incubation of nuclei with proteases coupled to agarose removed NLS-binding protein activity. Extracts enriched for NLS-binding proteins can be added back to salt or protease-treated nuclei to restore NLS-binding activity. These results suggest that the first step of nuclear protein import can be reconstituted in vitro.
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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.