Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
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DOI：
10.1126/science.273.5282.1717
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发表时间：
1996-09-20
期刊：
影响因子：
56.9
通讯作者：
Maniatis, T
中科院分区：
文献类型：
--
作者：
Kim, TK;Maniatis, T
STAT蛋白(信号转导和转录激活子)是一种潜在的细胞质转录因子，可被Janus激酶磷酸化以响应细胞因子。磷酸化的STAT蛋白转移到细胞核，在那里它们瞬间启动特定的细胞因子诱导基因集。控制激活的STAT蛋白数量的机制尚不清楚。在HeLa细胞中，干扰素-伽马处理激活的STAT1蛋白被蛋白酶体抑制剂稳定，并在体内泛素化。因此，激活的STAT1的数量可能受到泛素-蛋白酶体途径的负调控。
STAT proteins (signal transducers and activators of transcription) are latent cytoplasmic transcription factors that are phosphorylated by Janus kinases in response to cytokines. Phosphorylated STAT proteins translocate to the nucleus, where they transiently turn on specific sets of cytokine-inducible genes. The mechanism that controls the amounts of activated STAT proteins is not understood. STAT1 proteins activated by interferon-gamma treatment in HeLa cells were shown to be stabilized by a proteasome inhibitor and ubiquitinated in vivo. Thus, the amount of activated STAT1 may be negatively regulated by the ubiquitin-proteasome pathway.