INTERFERON-DEPENDENT TYROSINE PHOSPHORYLATION OF A LATENT CYTOPLASMIC TRANSCRIPTION FACTOR

INTERFERON-DEPENDENT TYROSINE PHOSPHORYLATION OF A LATENT CYTOPLASMIC TRANSCRIPTION FACTOR
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DOI:
10.1126/science.1496401
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发表时间:
1992-08-07
期刊:
影响因子:
56.9
通讯作者:
DARNELL, JE
DARNELL, JE
中科院分区:
综合性期刊1区
文献类型:
--
作者:
SCHINDLER, C;SHUAI, K;DARNELL, JE

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干扰素-α刺激的基因因子3(ISGF3)是一种转录激活剂,含有三种蛋白质,称为ISGF3-α蛋白,它们驻留在细胞质中,直到它们被干扰素-α激活。用干扰素-α处理细胞,导致这三种蛋白在酪氨酸上被磷酸化,并移位到细胞核,在那里它们通过与干扰素-α刺激的DNA反应元件结合来刺激转录。干扰素-γ通过不同的受体和不同的DNA结合部位激活转录,也导致其中一种蛋白质的酪氨酸磷酸化。ISGF3-α蛋白可能是配体结合到细胞表面激活的一个或多个激酶的底物,并可能将特定多肽受体的占据与一组特定基因的转录激活联系在一起。
The interferon-alpha (IFN-alpha)-stimulated gene factor 3 (ISGF3), a transcriptional activator, contains three proteins, termed ISGF3-alpha-proteins,that reside in the cell cytoplasm until they are activated in response to IFN-alpha. Treatment of cells with IFN-alpha caused these three proteins to be phosphorylated on tyrosine and to translocate to the cell nucleus where they stimulate transcription through binding to IFN-alpha-stimulated response elements in DNA. IFN-gamma, which activates transcription through a different receptor and different DNA binding sites, also caused tyrosine phosphorylation of one of these proteins. The ISGF3-alpha-proteins may be substrates for one or more kinases activated by ligand binding to the cell surface and may link occupation of a specific polypeptide receptor with activation of transcription of a set of specific genes.