ArticleThe Journal of cell biology1992
A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 61 citations in OpenAlex.
- 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 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
- Differential roles of heat shock protein 70 in the in vitro nuclear import of glucocorticoid receptor and simian virus 40 large tumor antigen.Molecular and cellular biology · 1994Article
- Nucleocytoplasmic transport.The Biochemical journal · 1994Review
- Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope.The Journal of cell biology · 1994Article
- The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals.The Plant cell · 1994Article
- Nuclear Ca2+ concentration measured with specifically targeted recombinant aequorin.The EMBO journal · 1993Article
- 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
- Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins.The Journal of cell biology · 1992Article
- Chromosome condensation caused by loss of RCC1 function requires the cdc25C protein that is located in the cytoplasm.Molecular biology of the cell · 1992Article
- A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.The EMBO journal · 1992Article
- Nuclear targeting in plants.Plant physiology · 1992Article
- A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast.Molecular biology of the cell · 1992Article
- In vitro nucleo-cytoplasmic transport.Molecular biology reportsArticle
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have purified proteins of 70 kD from Drosophila, HeLa cells, and Z. mays that specifically bind nuclear localization sequences (NLSs). These proteins are recognized by antibodies raised against a previously identified NLS-binding protein (NBP) from the yeast S. cerevisiae. All NBPs are associated with nuclei and also present in the cytosol. NBPs are phosphorylated and phosphatase treatment abolished NLS binding. The requirement for NBPs in nuclear protein uptake is demonstrated in semipermeabilized Drosophila melanogaster tissue culture cells. Proper import of a fluorescent protein containing the large T antigen NLS requires cytosol and ATP. In the absence of cytosol and/or ATP, NLS-containing proteins are bound to cytosolic structures and the nuclear envelope. Addition of cytosol and ATP results in movement of this bound intermediate into the nucleus. Anti-NBP antibodies specifically inhibited the binding part of this import reaction. These results indicate that a phosphoprotein common to several eukaryotes acts as a receptor that recognizes NLSs before their uptake into the nucleus.
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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.