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mTOR-dependent regulation of ribosomal gene transcription requires S6K1 and is mediated by phosphorylation of the carboxy-terminal activation domain of the nucleolar transcription factor UBF 总被引:2,自引:0,他引:2
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Hannan KM Brandenburger Y Jenkins A Sharkey K Cavanaugh A Rothblum L Moss T Poortinga G McArthur GA Pearson RB Hannan RD 《Molecular and cellular biology》2003,23(23):8862-8877
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D J O'Mahony W Q Xie S D Smith H A Singer L I Rothblum 《The Journal of biological chemistry》1992,267(1):35-38
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J H van Laar C A Berrevoets J Trapman N D Zegers A O Brinkmann 《The Journal of biological chemistry》1991,266(6):3734-3738
Phosphorylation of the androgen receptor was investigated in the absence of hormone as well as during and after transformation of the receptor to the tight nuclear binding form. Human prostate tumor cells (LNCaP) were labeled for 4 h with [32P]orthophosphate in the presence or absence of steroid. Subsequently, androgen receptors were immunoprecipitated either from total cell lysates or from nuclear extracts using a specific monoclonal antibody. The immunoprecipitated receptor preparations were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western blotting, using a polyclonal antiserum, and autoradiography. It was observed that the androgen receptor is already phosphorylated in the absence of hormone, but undergoes a hormone-induced additional phosphorylation. After administration of 10 nM R1881, a 1.8-fold increase in phosphorylation over nonstimulated control cells was reached. Moreover, the amount of nuclear extractable androgen receptor was increased; the acquisition of tight nuclear binding capacity was accompanied by hormone-induced receptor phosphorylation. 相似文献
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