小热休克蛋白的结构和功能

被引：61

作者：

夏佳音

张耀洲

机构：

[1] 浙江理工大学生物化学研究所

来源：

中国生物化学与分子生物学报 | 2007年 / 11期

关键词：

小热休克蛋白; 结构特征; 磷酸化作用; 低聚体; 底物;

D O I：

10.13865/j.cnki.cjbmb.2007.11.010

中图分类号：

Q51 [蛋白质];

学科分类号：

070307 [化学生物学];

摘要：

小热休克蛋白(small heat shock protein,sHSP)几乎存在于所有生物体中,其主要结构是一个保守的α晶体蛋白(α-crystallin)结构域,由约90个氨基酸残基组成,与其相邻的是可变的N端域.N端域能够调节低聚体形成、亚单位动力学及其与底物的结合.sHSP能够与细胞内各组分(蛋白质、细胞核、细胞骨架元件、膜)进行相互作用,以维持细胞的稳定.小热休克蛋白家族成员的共同特点是特殊丝氨酸残基上的磷酸化,磷酸化作用对于受到胁迫时的细胞非常重要.由MAPKAP激酶2/3和p38参与的级联反应能够诱导sHSP发生磷酸化,从而调节sHSP的低聚体状态,而低聚体状态和sHSP的生物学功能密切相关.本文介绍sHSP的结构特征和细胞内的作用底物,并讨论sHSP被不同的蛋白激酶磷酸化及磷酸化作用对低聚体状态和伴侣活性的影响.

引用

收藏

页码：911 / 915

页数：5

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