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• W2022731471 endingPage "377" @default.
• W2022731471 startingPage "373" @default.
• W2022731471 abstract "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 NH2- 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." @default.
• W2022731471 created "2016-06-24" @default.
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• W2022731471 date "2008-08-01" @default.
• W2022731471 modified "2023-10-06" @default.
• W2022731471 title "ARA24/Ran enhances the androgen-dependent NH2- and COOH-terminal interaction of the androgen receptor" @default.
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• W2022731471 doi "https://doi.org/10.1016/j.bbrc.2008.06.024" @default.
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