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

Autophagy. 2013 Dec;9(12):1937-54. doi: 10.4161/auto.26448. Epub 2013 Oct 8.


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.

Keywords: HSC70; P140 peptide; X-ray structure; autophagy; lupus; nucleotide exhange factor.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Anti-Bacterial Agents / therapeutic use
  • Antineoplastic Agents / therapeutic use
  • Autophagy*
  • HSC70 Heat-Shock Proteins* / antagonists & inhibitors
  • HSC70 Heat-Shock Proteins* / chemistry
  • HSC70 Heat-Shock Proteins* / physiology
  • Humans
  • Immunity / genetics
  • Immunosuppressive Agents / therapeutic use
  • Models, Molecular
  • Molecular Targeted Therapy
  • Protein Conformation
  • Structure-Activity Relationship


  • Anti-Bacterial Agents
  • Antineoplastic Agents
  • HSC70 Heat-Shock Proteins
  • Immunosuppressive Agents