Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt.
Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt.
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DOI：
10.1126/science.278.5338.687
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发表时间：
1997-10
期刊：
影响因子：
56.9
通讯作者：
L. Peso;M. González‐García;C. Page;R. Herrera;G. Núñez
中科院分区：
文献类型：
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作者：
L. Peso;M. González‐García;C. Page;R. Herrera;G. Núñez
BAD是促进细胞死亡的Bcl-2家族的远亲成员。BAD的磷酸化阻止了这一点。白细胞介素3（IL 3）诱导的BAD磷酸化可被磷脂酰肌醇3激酶（PI 3-kinase）特异性抑制剂抑制。Akt是一种促进生存的丝氨酸-苏氨酸蛋白激酶，IL-3以PI 3激酶依赖的方式激活Akt。发现Akt的活性而非活性形式在体内和体外在响应于IL-3而磷酸化的相同残基处磷酸化BAD。因此，BAD的促凋亡功能由PI 3-激酶-Akt途径调节。
BAD is a distant member of the Bcl-2 family that promotes cell death. Phosphorylation of BAD prevents this. BAD phosphorylation induced by interleukin-3 (IL-3) was inhibited by specific inhibitors of phosphoinositide 3-kinase (PI 3-kinase). Akt, a survival-promoting serine-threonine protein kinase, was activated by IL-3 in a PI 3-kinase-dependent manner. Active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3. Thus, the proapoptotic function of BAD is regulated by the PI 3-kinase-Akt pathway.