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E3泛素连接酶Itch在T细胞活化、分化及耐受性中的作用

The E3 ubiquitin ligase Itch in T cell activation, differentiation, and tolerance.

作者信息

Liu Yun-Cai

机构信息

Division of Cell Biololgy, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.

出版信息

Semin Immunol. 2007 Jun;19(3):197-205. doi: 10.1016/j.smim.2007.02.003. Epub 2007 Apr 11.

Abstract

Tagging a small molecule ubiquitin to a protein substrate, or protein ubiquitination, plays an important role in the immune responses. This process is catalyzed by a cascade of enzymatic reactions, with the E3 ubiquitin ligases being the critical enzymes that determine the specificity of substrate recognition. The E3 ligase Itch was identified from a mutant mouse which displays skin scratching and abnormal immune disorders. In the past few years, much progress has been made in our understanding of Itch-promoted protein ubiquitination, modulation of its ligase activity by upstream kinases, and the kinase-ligase interaction in T cell differentiation and tolerance induction.

摘要

将小分子泛素标记到蛋白质底物上,即蛋白质泛素化,在免疫反应中发挥着重要作用。这个过程由一系列酶促反应催化,其中E3泛素连接酶是决定底物识别特异性的关键酶。E3连接酶Itch是从一只表现出皮肤瘙痒和异常免疫紊乱的突变小鼠中鉴定出来的。在过去几年里,我们对Itch促进的蛋白质泛素化、上游激酶对其连接酶活性的调节以及T细胞分化和耐受性诱导中的激酶-连接酶相互作用的理解取得了很大进展。

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