ARA24/Ran enhances the androgen-dependent NH2- and COOH-terminal interaction of the androgen receptor.
Biochem Biophys Res Commun
; 373(3): 373-7, 2008 Aug 29.
Article
en En
| MEDLINE
| ID: mdl-18565325
The androgen receptor (AR) acts as an androgen-dependent transcription factor controlling the development of prostate tissue. Upon binding to androgen, AR undergoes a dynamic structural change leading to interaction between the NH(2)- and COOH-terminal regions of AR (N-C interaction). ARA24/Ran, which is a small GTPase, functions as an AR coactivator. Here, we report that ARA24/Ran enhances the N-C interaction of AR. The constitutively GTP- or GDP-bound form of ARA24/Ran repressed the AR N-C interaction. ARA24/Ran did not enhance the transcriptional activities of AR mutants that disrupt the N-C interaction. ARA24/Ran formed an endogenous protein complex with nuclear AR, but not cytoplasmic AR. Unlike SRC-1 with the positive activity for AR N-C interaction, ARA24/Ran did not enhance the transcriptional activity of the COOH-terminal domain-deleted AR mutant that is constitutively localized in the nucleus. These data demonstrate that ARA24/Ran increases AR transactivation by enhancing the AR N-C interaction in the nucleus.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Receptores Androgénicos
/
Proteína de Unión al GTP ran
/
Andrógenos
Límite:
Humans
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Male
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2008
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos