The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor
Open accessAbstract
The vertebrate glucocorticoid receptor (GR) is cytoplasmic without hormone and localizes to the nucleus after hormone binding. GR has two nuclear localization signals (NLS): NL1 is similar in sequence to the SV40 NLS; NL2 is poorly defined, residing in the ligand-binding domain. We found that GR displayed similar hormone-regulated compartmentalization in Saccharomyces cerevisiae and required the Sxm1 nuclear import receptor for NL2-mediated import. Two metazoan homologues of Sxm1, importin 7 and importin 8, bound both NL1 and NL2, whereas importin α selectively bound NL1. In an in vitro nuclear import assay, both importin 7 and the importin α-importin β heterodimer could import a GR NL1 fragment. Under these conditions, full-length GR localized to nuclei in the presence but not absence of an unidentified component in cell extracts. Interestingly, importin 7, importin 8, and importin α bound GR even in the absence of hormone; thus, hormonal control of localization is exerted at a step downstream of import receptor binding.
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Cites
Galigniana, M. D., Radanyi, C., Renoir, J.-M., Housley, P. R., & Pratt, W. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010809200 · Cited by 236 · cited 1×
“Pratt and colleagues have demonstrated that components of the apoGR complex bind cytoskeletal factors (Galigniana et al., 2001).”
Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.14.4.422 · Cited by 168 · cited 1×
“Molecular chaperone complexes interact with GR and other intracellular receptors to facilitate hormone binding (Dittmar and Pratt, 1997) and the disassembly of GR-containing transcriptional regulatory complexes (Freeman et al., 2000).”
BackgroundSelf-citation
Cited by
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423
Oakley, R. H., & Cidlowski, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.179325 · Cited by 373
Busillo, J. M., & Cidlowski, J. A. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.11.005 · Cited by 339
Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298
Self-citationGlucocorticoids sensitize the innate immune system through regulation of the NLRP3 inflammasome
Busillo, J. M., Azzam, K. M., & Cidlowski, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275370 · Cited by 264
Metadata
- Authors
- Freedman, N. D., & Yamamoto, K. R.
- Venue
- Molecular Biology of the Cell
- Published
- 2004-05
- Volume
- 15
- Issue
- 5
- Pages
- 2276-2286
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2096774529
- Cited by
- 213
- References
- 2
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- green
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- Freedman, N. D., & Yamamoto, K. R. (2004). Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e03-11-0839
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