协同伴侣分子CHIP的E3连接酶活性及其生物学意义

E3 Ligase Activity of CHIP,a Cochaperones and Its Biological Significance

CHIP(carboxy terminus of Hsc70 interacting protein)是一种新发现的具有泛素化连接酶活性的协同分子伴侣,它N端有TPR(the tetratricopeptide repeat)结构,可以和分子伴侣结合,C端有U-box结构,具有E3酶功能。CHIP可以介导一系列重要蛋白质的泛素化降解,从而维持细胞内蛋白质的质量。现就CHIP的结构和功能、CHIP的底物特征、CHIP的生物学作用以及CHIP在疾病发生中的可能作用做一综述。

CHIP, carboxy terminus of Hsc70 interacting protein, is a new co-chaperone with E3 ligase activity discovered recently. It had the tetratricopeptide repeat （TPR） domain at its amino terminus and could interact with chaperones, and it had E3 ligase activity with a U-box domain at its carboxy terminus. CHIP could play a E3 ligase role during a series of protein degradation to control proteins quality in the cell. The structure and ability, client substrates, biological characterization and roles in illness of CHIP were reviewed in this paper.