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Janus激酶(JAKs)以及信号转导子和转录激活子(STATs)的结构、调控与功能。

The structure, regulation and function of the Janus kinases (JAKs) and the signal transducers and activators of transcription (STATs).

作者信息

Pellegrini S, Dusanter-Fourt I

机构信息

INSERM U276, Institut Pasteur, Paris, France.

出版信息

Eur J Biochem. 1997 Sep 15;248(3):615-33. doi: 10.1111/j.1432-1033.1997.00615.x.

DOI:10.1111/j.1432-1033.1997.00615.x
PMID:9342212
Abstract

Since the discovery of their physiological roles in cytokine signalling, the Janus kinases (JAKs) and the signal transducers and activators of transcription (STATs) have attracted considerable attention, to the point that the concept of a intracellular signalling pathway, named JAK/STAT, has emerged. As originally defined, this pathway involves ligand-dependent activation of a particular class of receptor-associated tyrosine kinases, the JAK proteins, which phosphorylate themselves and receptor components, creating recruitment sites for STAT transcription factors. The STATs are phosphorylated, they dissociate from the receptor x JAK complex and translocate to the nucleus where they participate in transcriptional gene activation. Although this pathway was found initially to be activated by interferons, it is now known that a large number of cytokines, growth factors and hormonal factors activate JAK and/or STAT proteins. Recent findings have suggested that the interdependence of JAKs and STATs might not be absolute as originally thought.

摘要

自从发现Janus激酶(JAKs)和信号转导子及转录激活子(STATs)在细胞因子信号传导中的生理作用以来,它们已引起了相当大的关注,以至于出现了一种名为JAK/STAT的细胞内信号传导途径的概念。按照最初的定义,该途径涉及一类特定的受体相关酪氨酸激酶(即JAK蛋白)的配体依赖性激活,这些JAK蛋白会自身磷酸化以及使受体成分磷酸化,从而为STAT转录因子创造募集位点。STATs被磷酸化后,它们从受体 - JAK复合物上解离并转移至细胞核,在那里它们参与转录基因的激活。尽管最初发现该途径是由干扰素激活的,但现在已知大量的细胞因子、生长因子和激素因子均可激活JAK和/或STAT蛋白。最近的研究结果表明,JAKs和STATs之间的相互依赖性可能并不像最初认为的那样绝对。

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