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Domains of the Human Androgen Receptor Involved in Steroid Binding, Transcriptional Activation, and Subcellular Localization
Open accessAbstract
A series of human androgen receptor (AR) deletion mutants was constructed to study the relationship between the structural domains and their different functions in the AR protein. Human AR mutants were expressed in COS-1 and HeLa cells to investigate hormone binding, transcriptional activation, and subcellular localization. The wild-type human AR (AR 1–910) was expressed as a 110- to 112-kDa doublet, as revealed on immunoblots. All mutant AR proteins also migrated as doublets, except for one. This AR has a deletion from amino acid residues 51–211 and migrated as a single protein band, possibly due to altered posttranslational modification. The AR steroid-binding domain is encoded by approximately 250 amino acid residues in the Cterminal end. Deletions in this domain as well as truncation of the last 12 C-terminal amino acid residues abolished hormone binding. Cotransfection studies in HeLa cells showed that transcriptional activation of an androgen-regulated reporter gene construct was induced by the wildtype human AR. Mutational analysis revealed two regions in the N-terminal part, encoded by amino acid residues 51–211 and 244–360, to be essential for this transcriptional activation. Deletion of the hormone-binding domain yielded a constitutively active AR protein, indicating that in the absence of hormone this domain displays an inhibitory function. In the presence of its ligand, the wild-type AR was located in the cell nucleus. In the absence of androgens the receptor was mainly nuclear, but cytoplasmic localization was observed as well. In contrast, an AR deletion mutant lacking part of the DNAbinding domain and part of the hinge region was exclusively cytoplasmic in the absence of hormone. This mutant AR lacks a region that is highly conserved among steroid receptors and homologous to the simian virus-40 large T-antigen- and nucleoplas-min-nuclear localization signals. Transformation by hormone directed this mutant to the nucleus, indicating the presence of a second, hormone-dependent nuclear targeting mechanism.
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“AF-2 deletion mutants of AR or AR splicing variants lacking LBD still possess potent transcription activation functions (Guo et al., 2009; Jenster et al., 1995; Jenster et al., 1991; Simental et al., 1991).”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as Jenster et al., 1991
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Linja, M. J., & Visakorpi, T. (2004) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2004.10.012 · Cited by 154
Ruff, M., Gangloff, M., Wurtz, J., & Moras, D. (2000) · Breast Cancer Research · doi:10.1186/bcr80 · Cited by 153
Ligand-dependent inhibition of β-catenin/TCF signaling by androgen receptor
Chesire, D. R., & Isaacs, W. B. (2002) · Oncogene · doi:10.1038/sj.onc.1206049 · Cited by 151
“That unliganded AR can be found in both the cytosol and nucleus (Husmann et al., 1990; Jenster et al., 1991) implies AR target gene expression is not solely dependent on nuclear localization, but also hitherto uncharacterized nuclear events.”
BackgroundMolecular Mechanisms of Androgen Action
Lindzey, J. K., Kumar, M. V., Grossman, M., Young, C. Y. F., & Tindall, D. J. (1994) · Vitamins and hormones · doi:10.1016/s0083-6729(08)61151-6 · Cited by 148
Small Molecule Inhibitors Targeting the “Achilles' Heel” of Androgen Receptor Activity
Sadar, M. D. (2011) · Cancer Research · doi:10.1158/0008-5472.can_10-3398 · Cited by 151
Willson, T. M., Henke, B. R., Momtahen, T. M., Charifson, P. S., Batchelor, K. W., Lubahn, D. B., Moore, L. B., Oliver, B. B., Sauls, H. R., Triantafillou, J. A., et al. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00037a002 · Cited by 146
Conformational Analysis of the Androgen Receptor Amino-terminal Domain Involved in Transactivation
Reid, J., Kelly, S. M., Watt, K., Price, N. C., & McEwan, I. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201003200 · Cited by 143
Cyclin D1: Mechanism and Consequence of Androgen Receptor Co-repressor Activity
Petre, C. E., Wetherill, Y. B., Danielsen, M., & Knudsen, K. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106399200 · Cited by 144
Trinucleotide repeats in the human androgen receptor: a molecular basis for disease
Choong, C. S., & Em, W. (1998) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0210235 · Cited by 141
Repressors of Androgen and Progesterone Receptor Action
Agoulnik, I. U., Krause, W. C., Bingman, W. E., Rahman, H., Amrikachi, M., Ayala, G. E., & Weigel, N. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305153200 · Cited by 141
Veldscholte, J., Berrevoets, C. A., Zegers, N. D., Van der Kwast, T. H., Grootegoed, J. A., & Mulder, E. (1992) · Biochemistry · doi:10.1021/bi00147a029 · Cited by 139
Decoding the androgen receptor splice variants.
Lu, C., & Luo, J. (2013) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2223-4683.2013.09.08 · Cited by 138
“Such variants have the potential to mediate constitutively active AR function, on the basis of earlier in vitro studies on AR deletion constructs generated in the laboratory (22).”
BackgroundAndrogen Receptor Interacts with a Novel MYST Protein, HBO1
Sharma, M., Zarnegar, M. A., Li, X., Lim, B., & Sun, Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004838200 · Cited by 137
Androgen Receptor Mutations in Prostate Cancer
Gelmann, E. P. (1996) · Cancer treatment and research · doi:10.1007/978-1-4613-1267-3_12 · Cited by 136
Hey1, a Mediator of Notch Signaling, Is an Androgen Receptor Corepressor
Belandia, B., Powell, S. M., Garcia-Pedrero, J. M., Walker, M. M., Bevan, C. L., & Parker, M. G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1425-1436.2005 · Cited by 137
“COS-1 cells were cotransfected with 20 ng of TAT-GRE-E1B-LUC, expression vectors for AR(1-653) (5 ng) and SRC1e (10 ng), and increasing amounts of the Hey1 expression vector (5, 10, or 20 ng).”
MethodDalal, K., Roshan‐Moniri, M., Sharma, A., Li, H., Ban, F., Hessein, M., Hsing, M., Singh, K., Leblanc, E., Dehm, S. M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.553818 · Cited by 135
“The AR structural organization includes an N-terminal domain (NTD), followed by the DBD and LBD domains (6).”
BackgroundPosttranslational Modification of the Androgen Receptor in Prostate Cancer
der Steen, T. V., Tindall, D. J., & Huang, H. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714833 · Cited by 140
“majority of AR activity [52–54].”
Evidence for Calpain-Mediated Androgen Receptor Cleavage as a Mechanism for Androgen Independence
Libertini, S. J., Tepper, C. G., Rodriguez, V., Asmuth, D. M., Kung, H.-J., & Mudryj, M. M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1072 · Cited by 129
“Previous reports show that deletion of the LBD generates an androgen-independent transcriptional activator (7).”
Androgen Receptor Antagonists in Castration-Resistant Prostate Cancer
Rathkopf, D. E., & Scher, H. I. (2013) · The Cancer Journal · doi:10.1097/ppo.0b013e318282635a · Cited by 131
“Because first- and second-generation antiandrogens bind to the C-terminal LBD, newer methods of targeting the AR include targeting the regulatory N-terminal domain, which is essential for transcription in the presence or absence of ligand.(57) EPI-001 is a novel, small molecule peptide that binds to the N-terminus and…”
BackgroundKuil, C. W., Berrevoets, C., & Mulder, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.46.27569 · Cited by 130
Metadata
- Authors
- Jenster, G., van der Korput, H. A. G. M., van Vroonhoven, C., van der Kwast, T. H., Trapman, J., & Brinkmann, A. O.
- Affiliations
- Erasmus University Rotterdam (NL)
- ORCID
- Jenster, Guido
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1991-10
- Volume
- 5
- Issue
- 10
- Pages
- 1396-1404
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W2002791165
- Cited by
- 523
- References
- 52
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 13 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 12 · 2019: 11 · 2018: 15 · 2017: 16 · 2016: 18 · 2015: 12 · 2014: 14 · 2013: 17 · 2012: 18
- FWCI
- 25.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Prostate Cancer Treatment and Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal and reproductive studies
- Keywords
- androgen receptor, steroid-binding domain, transcriptional activation, subcellular localization, nuclear localization signal, nuclear targeting, hormone binding, constitutively active receptor, deletion mutants, DNA-binding domain, hinge region, post-translational modification
- MeSH terms
- Animals, Binding Sites, Cell Line, Chromosome Deletion, DNA-Binding Proteins, Genetic Vectors, HeLa Cells, Humans, Immunohistochemistry, Plasmids, Receptors, Androgen, Recombinant Proteins, Transcription, Genetic, Transfection, Restriction Mapping, Chloramphenicol O-Acetyltransferase, Metribolone
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