HSPA8/HSC70 chaperone protein: Structure, function, and chemical targeting

François Stricher, Christophe Macri, Marc Ruff, Sylviane Muller

Research output: Contribution to journalReview ArticleResearchpeer-review

121 Citations (Scopus)

Abstract

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively expressed, cognate protein of the HSP70 family, which is central in many cellular processes. In particular, its regulatory role in autophagy is decisive. We focused this review on HSC70 structure-function considerations and based on this, we put a particular emphasis on HSC70 targeting by small molecules and peptides in order to develop intervention strategies that deviate some of HSC70 properties for therapeutic purposes. Generating active biomolecules regulating autophagy via its effect on HSC70 can effectively be designed only if we understand the fine relationships between HSC70 structure and functions.

Original languageEnglish
Pages (from-to)1937-1954
Number of pages18
JournalAutophagy
Volume9
Issue number12
DOIs
Publication statusPublished - Dec 2013
Externally publishedYes

Keywords

  • Autophagy
  • HSC70
  • Lupus
  • Nucleotide exhange factor
  • P140 peptide
  • X-ray structure

Cite this