Structural and functional analysis of the Hsp70/Hsp40 chaperone system

Research output: Contribution to journalReview article


External Institution(s)

  • Virginia Commonwealth University
  • Hebei Medical University


Original languageEnglish (US)
Pages (from-to)378-390
Number of pages13
JournalProtein Science
Issue number2
StatusPublished - Feb 1 2020


As one of the most abundant and highly conserved molecular chaperones, the 70-kDa heat shock proteins (Hsp70s) play a key role in maintaining cellular protein homeostasis (proteostasis), one of the most fundamental tasks for every living organism. In this role, Hsp70s are inextricably linked to many human diseases, most notably cancers and neurodegenerative diseases, and are increasingly recognized as important drug targets for developing novel therapeutics for these diseases. Hsp40s are a class of essential and universal partners for Hsp70s in almost all aspects of proteostasis. Thus, Hsp70s and Hsp40s together constitute one of the most important chaperone systems across all kingdoms of life. In recent years, we have witnessed significant progress in understanding the molecular mechanism of this chaperone system through structural and functional analysis. This review will focus on this recent progress, mainly from a structural perspective.

    Research areas

  • Hsp40, Hsp70, molecular chaperone, neurodegenerative diseases, protein folding, proteostasis