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Background
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Androgen receptor (ANDR) has 3 major functional domains: the N-terminal domain, DNA-binding domain, and an androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. The gene for this protein contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of the protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations are also associated with complete androgen insensitivity (CAIS). PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor; sumoylation of ANDR represses androgen receptor dependent transcription.
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Background
References
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- Nishida, et al. J. Biol. Chem. 277 (44), 41311-41317 (2002)
- Sills, E.S., et al., Int. J. Mol. Med. 9(1):45-48 (2002).
- Chavez, B., et al., J. Hum. Genet. 46(10):560-565 (2001).
- Ahmed, S.F., et al., J. Clin. Endocrinol. Metab. 85(2):658-665 (2000).
- Marcelli, M., et al., Cancer Res. 60(4):944-949 (2000).
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