Hsp90 Chaperone Complex Assembly and the Regulation to Steroid Receptors

Abstract: 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.

CSTR: 32200.14.cjcb.2006.01.0002