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.
journal_name
Cellsjournal_title
Cellsauthors
Bonam SR,Ruff M,Muller Sdoi
10.3390/cells8080849subject
Has Abstractpub_date
2019-08-07 00:00:00issue
8issn
2073-4409pii
cells8080849journal_volume
8pub_type
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