Fiche publication
Date publication
août 2019
Journal
Cells
Auteurs
Membres identifiés du Cancéropôle Est :
Pr MULLER Sylviane
,
Dr RUFF Marc
Tous les auteurs :
Bonam SR, Ruff M, Muller S
Lien Pubmed
Résumé
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.
Mots clés
HSPA8/HSC70, P140, autoimmune diseases, chaperone-mediated autophagy, lysosomes, pharmacological regulators, systemic lupus erythematosus
Référence
Cells. 2019 Aug 7;8(8):
