ArticleProceedings of the National Academy of Sciences of the United States of America1994
Nuclear localization signals also mediate the outward movement of proteins from the nucleus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Membrane-Initiated Estrogen, Androgen, and Progesterone Receptor Signaling in Health and Disease.Endocrine reviews · 2022Review
- The Role of Progesterone Receptors in Breast Cancer.Drug design, development and therapy · 2022Review
- Dissecting in vivo steady-state dynamics of karyopherin-dependent nuclear transport.Molecular biology of the cell · 2016Article
- Progesterone receptor isoforms PRA and PRB differentially contribute to breast cancer cell migration through interaction with focal adhesion kinase complexes.Molecular biology of the cell · 2013Article
- Hormone-dependent nuclear export of estradiol receptor and DNA synthesis in breast cancer cells.The Journal of cell biology · 2008Article
- Regulation of SRC-3 intercompartmental dynamics by estrogen receptor and phosphorylation.Molecular and cellular biology · 2007Article
- Estrogen-induced loss of progesterone receptor expression in normal and malignant ovarian surface epithelial cells.Oncogene · 2005Article
- Import and export of nuclear proteins: focus on the nucleocytoplasmic movements of two different species of mammalian estrogen receptor.Molecular and cellular biochemistry · 2004Review
- Heat shock protein 90 and the nuclear transport of progesterone receptor.Cell stress & chaperones · 2001Article
- Article
- Discrimination between NL1- and NL2-mediated nuclear localization of the glucocorticoid receptor.Molecular and cellular biology · 1999Article
- RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear export.The Journal of cell biology · 1997Article
- Promoter- and cell-specific responses to sex steroids.Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA · 1997Review
- ATP-dependent release of glucocorticoid receptors from the nuclear matrix.Molecular and cellular biology · 1996Article
- Protein export from the nucleus requires the GTPase Ran and GTP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- mRNA transport in yeast: time to reinvestigate the functions of the nucleolus.Molecular biology of the cell · 1995Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several nuclear proteins, including steroid hormone receptors, have been shown to shuttle continuously between the nucleus and the cytoplasm. The mechanism of entry of proteins into the nucleus is well documented, whereas the mechanism of their outward movement into the cytoplasm is not understood. We have grafted the nuclear localization signals of the progesterone receptor or the simian virus 40 large tumor antigen onto beta-galactosidase. These additions were shown to impart to the protein the ability to shuttle between the nucleus and the cytoplasm. Microinjected proteins devoid of a nuclear localization signal were unable to exit from the nucleus. The same nuclear localization signals are thus involved in both the inward and the outward movement of proteins through the nuclear membrane. We also show that although the nuclear import requires energy, the nuclear export does not. These results suggest that the nucleocytoplasmic shuttling may be a general phenomenon for nuclear proteins that could possibly undergo modifications in the cytoplasm and exert some biological activities there. These conclusions also imply that at least part of the cellular machinery involved in the nuclear import of proteins may function bidirectionally.
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