Mechanisms for regulation of Hsp70 function by Hsp40

AUTOR(ES)

Fan, Chun-Yang

FONTE

Cell Stress Society International

RESUMO

The Hsp70 family members play an essential role in cellular protein metabolism by acting as polypeptide-binding and release factors that interact with nonnative regions of proteins at different stages of their life cycles. Hsp40 cochaperone proteins regulate complex formation between Hsp70 and client proteins. Herein, literature is reviewed that describes the mechanisms by which Hsp40 proteins interact with Hsp70 to specify its cellular functions.

Documentos Relacionados

• Role of the J-domain in the cooperation of Hsp40 with Hsp70
• Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
• The Mammalian Hsp40 ERdj3 Requires Its Hsp70 Interaction and Substrate-binding Properties to Complement Various Yeast Hsp40-dependent Functions*
• Regulation of HSP70 synthesis by messenger RNA degradation.
• Regulation of Transcription Factor Pdr1p Function by an Hsp70 Protein in Saccharomyces cerevisiae