Phosphorylation of the androgen receptor by a nuclear cAMP-independent protein kinase.
Phosphorylation of the androgen receptor by a nuclear cAMP-independent protein kinase.
复制标题
雄激素受体被核 cAMP 独立蛋白激酶磷酸化。
DOI：
10.1016/0006-291x(84)90297-3
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发表时间：
1984
影响因子：
3.1
通讯作者：
Ahmed,K
中科院分区：
文献类型：
--
作者：
Goueli,SA;Holtzman,JL;Ahmed,K
从大鼠腹侧前列腺中纯化雄激素受体。纯化的受体作为单分子带迁移。重量。 87000 在 SDS-聚丙烯酰胺凝胶上，R-1881（17 β-羟基-17α-甲基-estra-4,9,11-trien-3-one）结合的 Kd 为 6 nM，沉降系数为 4.5 S。通过在多种纯化蛋白激酶（包括 cAMP 依赖性蛋白）存在下将其与 [γ-32P]ATP 一起孵育来研究纯化受体的磷酸化激酶和四种不依赖 cAMP 的蛋白激酶（对卵黄高磷蛋白和酪蛋白等底物有活性）。 87000 mol 的磷酸化。重量。雄激素受体蛋白仅在存在核 cAMP 独立蛋白激酶（N2 型）的情况下出现。没有检测到受体的自身磷酸化。结果表明雄激素受体是一种磷蛋白。此外，雄激素受体仅被特定的核cAMP非依赖性蛋白激酶磷酸化对于确定其功能的动态可能很重要。
The androgen receptor was purified from rat ventral prostate. The purified receptor migrated as a single band of mol. wt. 87000 on SDS-polyacrylamide gels, had a Kdfor R-1881 (17 β-hydroxy-17α-methyl-estra-4,9,11-trien-3-one) binding as 6 nM, and sedimentation coefficient of 4.5 S. Phosphorylation of the purified receptor was studied by incubating it with [γ-32P]ATP in the presence of several purified protein kinases including cAMP-dependent protein kinase, and four cAMP-independent protein kinases (which were active towards substrates such as phosvitin and casein). Phosphorylation of the 87000 mol. wt. androgen receptor protein occurred only in the presence of a nuclear cAMP-independent protein kinase (of the N2 type). No auto-phosphorylation of the receptor was detected. The results indicate that the androgen receptor is a phosphoprotein. Further, phosphorylation of the androgen receptor by only a specific nuclear cAMP-independent protein kinase may be important in determining the dynamics of its function.