preprints.org > biology and life sciences > biochemistry and molecular biology > doi: 10.20944/preprints202012.0434.v1

Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 16 December 2020 / Approved: 17 December 2020 / Online: 17 December 2020 (12:46:28 CET)

Although cancers account for over 16% of all global deaths annually, at present, no reliable therapies exist for most types of the disease. As protein folding facilitators, heat shock proteins (Hsps) play an important role in cancer development. Not surprisingly, Hsps are among leading anticancer drug targets. Generally, Hsp70s are divided into two main subtypes: canonical Hsp70 (E. coli Hsp70/DnaK homologues) and the non-canonical (Hsp110 and Grp170) members. These two main Hsp70 groups are delineated from each other by distinct structural and functional specifications. Non-canonical Hsp70s are considered as holdase chaperones, while canonical Hsp70s are refoldases. This distinct characteristic feature is mirrored by the distinct structural features of these two groups of chaperones. Hsp110/Grp170 members are larger as they possess an extended acidic insertion in their substrate binding domains. While the role of canonical Hsp70s in cancer has received a fair share of attention, the roles of non-canonical Hsp70s in cancer development has received less attention in comparison. In the current review, we discuss the structure-function features of non-canonical Hsp70s members and how these features impact on their role in cancer development. We further mapped out their interactome and discussed the prospects of targeting these proteins in cancer therapy.

Hsp110; Grp170; non-canonical Hsp70; chaperone; cancer

Biology and Life Sciences, Biochemistry and Molecular Biology

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