期刊
CELLS
卷 8, 期 8, 页码 -出版社
MDPI
DOI: 10.3390/cells8080849
关键词
chaperone-mediated autophagy; HSPA8; HSC70; lysosomes; pharmacological regulators; P140; autoimmune diseases; systemic lupus erythematosus
类别
资金
- French Infrastructure for Integrated Structural Biology FRISBI [ANR-10-INBS-05]
- Instruct-ERIC
- Laboratory of Excellence Medalis [ANR-10-LABX-0034]
- TRANSAUTOPHAGY COST Action [CA15138]
- French club of Autophagy (CFATG)
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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