Frontiers in Structural Biology

Frontiers in Structural Biology

Role of Molecular Chaperones in Structural Folding, Biological Functions, and Drug Interactions of Client Proteins

The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological ...
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Mechanisms and Functions of the Cytosolic DNAJHsp70 Chaperone System

Pp. 214-250 (37)

Imad Baaklini and Jason C. Young

Abstract

The Hsp70 chaperone system is central to the proteostasis network in the cytosol of human cells. Hsp70 has roles in protein folding, the prevention and clearance of aggregates, and various other biological processes. A range of co-chaperone proteins regulate Hsp70, among these the Hsp40/DNAJ proteins are important activators of Hsp70 function. Stress inducible Hsp70 and its non-inducible form Hsc70 are ubiquitously expressed, and the most abundant DNAJs are DNAJA1 (Hdj2), DNAJA2 and DNAJB1 (Hsp40, Hdj1). Here, the mechanisms of Hsc70/Hsp70 with the DNAJs is reviewed. An overview of biological functions of the major DNAJs is then presented, particularly in the context of protein misfolding diseases.

Keywords:

DNAJ, Hsp40, Hsp70, Ion channel, Molecular chaperone, Neurodegeneration, Protein aggregation, Protein degradation, Protein folding.

Affiliation:

Department of Biochemistry, Groupe de Recherche Axe sur la Structure des Proteines, McGill University, Montreal, Canada.