Journal article
HSPA8/HSC70 chaperone protein: Structure, function, and chemical targeting
F Stricher, C Macri, M Ruff, S Muller
Autophagy | TAYLOR & FRANCIS INC | Published : 2013
DOI: 10.4161/auto.26448
Open access
Abstract
HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively expressed, cognate protein of the HSP70 family, which is central in many cellular processes. In particular, its regulatory role in autophagy is decisive. We focused this review on HSC70 structure-function considerations and based on this, we put a particular emphasis on HSC70 targeting by small molecules and peptides in order to develop intervention strategies that deviate some of HSC70 properties for therapeutic purposes. Generating active biomolecules regulating autophagy via its effect on HSC70 can effectively be designed only if we understand the fine relationships between HSC70 structure and functions..
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Funding Acknowledgements
We thank Jean-Paul Briand and Frederic Gros for helpful comments on the manuscript and Hayet Dali for excellent technical assistance. Research in the authors' laboratory is financially supported by the French Centre National de la Recherche Scientifique (CNRS), the Laboratory of Excellence Medalis, Initiative of Excellence (IdEx)/Strasbourg University, Region Alsace, and ImmuPharma France. Molecular graphics were performed with the UCSF Chimera package, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco.