Heat shock protein 110: A novel candidate for disease diagnosis and targeted therapy

Abstract

The heat shock protein 110 (Hsp110) family in eukaryotes plays a pivotal role in maintaining cellular proteostasis. As a unique class of molecular chaperones, Hsp110s act as both independent chaperones and cochaperones for other essential molecular chaperones. Malfunction of Hsp110s is involved in many diseases. Thus targeting Hsp110s or its interactions with client proteins may provide new approaches for developing therapeutics. In this review, we describe the current understanding of the role and molecular mechanism of Hsp110s in disease development, and discuss the recent exploration of Hsp110s as potential targets to provide a novel direction for disease diagnosis and targeted therapy.