HSPA8/HSC70 in immune disorders: A molecular rheostat that adjusts chaperone-mediated autophagy substrates

Srinivasa Reddy Bonam, Marc Ruff, Sylviane Muller

Research output: Contribution to journalReview articlepeer-review

31 Scopus citations

Abstract

HSPA8/HSC70 is a molecular chaperone involved in a wide variety of cellular processes. It plays a crucial role in protein quality control, ensuring the correct folding and re-folding of selected proteins, and controlling the elimination of abnormally-folded conformers and of proteins daily produced in excess in our cells. HSPA8 is a crucial molecular regulator of chaperone-mediated autophagy, as a detector of substrates that will be processed by this specialized autophagy pathway. In this review, we shortly summarize its structure and overall functions, dissect its implication in immune disorders, and list the known pharmacological tools that modulate its functions. We also exemplify the interest of targeting HSPA8 to regulate pathological immune dysfunctions.

Original languageEnglish (US)
Article number849
JournalCells
Volume8
Issue number8
DOIs
StatePublished - Aug 2019
Externally publishedYes

Keywords

  • Autoimmune diseases
  • Chaperone-mediated autophagy
  • HSPA8/HSC70
  • Lysosomes
  • P140
  • Pharmacological regulators
  • Systemic lupus erythematosus

ASJC Scopus subject areas

  • Medicine(all)

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