摘要
真核细胞中近100种蛋白质都受Hsp90的调节。这些蛋白质多与信号转导作用有关,它们与Hsp90一起进入一个以Hsp90/Hsp70为主的伴侣复合体,在复合体内完成信号转导作用。Hsp90除了和蛋白质的伴侣位点结合以外,还在其他位点与辅助因子连接,这是Hsp90能与蛋白质及辅助因子组装成复合体,并进而调节其信号作用的结构基础。类固醇受体等蛋白质的信号转导作用是在Hsp70、Hsp90为基础的5种蛋白质(Hsp90,Hsp70,Hop,Hsp40和p23)组成的复合体中进行的。这个系统可以帮助理解在真核细胞中,Hsp70和Hsp90怎样联合作用,改变底物蛋白构象,以及怎样应答信号作用。
Nearly 100 proteins are known to be regulated by Hsp90. Most of these proteins are involved in signal transduction, and they are brought into complex with Hsp90 by a multiprotein Hsp90/Hsp70-based chaperone machinery. In addition to binding substrate proteins at the chaperone sites, Hsp90 binds cofacters at other sites. This is the structure fundament for the heterocomplex assembly which regulate the signaling function. The signaling function of steroid receptors happens in the Hsp90/Hsp70-based five-proteins complex （Hsp90, Hsp70, Hop, Hsp40 and p23）. This system can facilitate understanding of how eukaryotic Hsp70 and Hsp90 work together as essential components of a process that alters the conformations of substrate proteins to states that respond in signal transduction.
出处
《细胞生物学杂志》
CAS
CSCD
2006年第1期5-10,共6页
Chinese Journal of Cell Biology
