HSPA8/HSC70 in Immune Disorders: A Molecular Rheostat that Adjusts Chaperone-Mediated Autophagy Substrates

Cells

Marc Ruff¹  Sylviane Muller²  SrinivasaReddy Bonam³ 

[1] peptide therapy, Biotechnology and cell signaling, CNRS-University of Strasbourg, Illkirch 67412, France/Laboratory of excellence Medalis, 67000 Strasbourg, France;Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404 Strasbourg, France;;Neuroimmunology &

关键词: chaperone-mediated autophagy;    HSPA8/HSC70;    lysosomes;    pharmacological regulators;    P140;    autoimmune diseases;    systemic lupus erythematosus;   

DOI  :  10.3390/cells8080849

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown