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

Cells
Srinivasa Reddy BonamSylviane Muller

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.

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Citations

Aug 31, 2019·International Journal of Molecular Sciences·Alijah A Griffith, William Holmes
Mar 26, 2021·Journal of Medicinal Chemistry·Junping PeiLiang Ouyang
Jun 3, 2021·Cells·Gabriela Rapozo GuimarãesMariana Boroni
Aug 8, 2021·International Journal of Molecular Sciences·Henrieta HavalováNina Kunová
Sep 30, 2021·Natural Products and Bioprospecting·Christian Bailly, Gérard Vergoten
Sep 19, 2021·The FEBS Journal·Akhouri Kishore RaghawanGhanshyam Swarup
Oct 10, 2021·Cellular and Molecular Life Sciences : CMLS·Bhavani S SahuAlessandro Bartolomucci

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