Next Article in Journal
The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae
Previous Article in Journal
Modulation of Agrin and RhoA Pathways Ameliorates Movement Defects and Synapse Morphology in MYO9A-Depleted Zebrafish
Article Menu

Export Article

Open AccessReview

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

1
Neuroimmunology & peptide therapy, Biotechnology and cell signaling, CNRS-University of Strasbourg, Illkirch 67412, France/Laboratory of excellence Medalis, 67000 Strasbourg, France
2
Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404 Strasbourg, France
3
University of Strasbourg Institute for Advanced Study (USIAS), 67000 Strasbourg, France
4
Fédération Hospitalo-Universitaire (FHU) OMICARE, Fédération de Médecine Translationnelle de Strasbourg (FMTS), Strasbourg University, 67000 Strasbourg, France
*
Author to whom correspondence should be addressed.
Cells 2019, 8(8), 849; https://doi.org/10.3390/cells8080849
Received: 19 July 2019 / Revised: 2 August 2019 / Accepted: 5 August 2019 / Published: 7 August 2019
(This article belongs to the Special Issue Chaperone-Mediated Autophagy)
  |  
PDF [3809 KB, uploaded 14 August 2019]
  |  

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. View Full-Text
Keywords: chaperone-mediated autophagy; HSPA8/HSC70; lysosomes; pharmacological regulators; P140; autoimmune diseases; systemic lupus erythematosus chaperone-mediated autophagy; HSPA8/HSC70; lysosomes; pharmacological regulators; P140; autoimmune diseases; systemic lupus erythematosus
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Bonam, S.R.; Ruff, M.; Muller, S. HSPA8/HSC70 in Immune Disorders: A Molecular Rheostat that Adjusts Chaperone-Mediated Autophagy Substrates. Cells 2019, 8, 849.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Cells EISSN 2073-4409 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top