Heat shock protein 110 (Hsp110)

Heat shock protein 110 is a large molecular chaperone found only in eukaryotes and is the largest member of the Hsp70 superfamily[1][2][7]. It consists of two main domains: a nucleotide-binding domain (NBD) at the amino terminus and a substrate-binding domain (SBD) at the carboxy terminus[1]. Unlike Hsp70, Hsp110 primarily acts as a holdase, efficiently preventing aggregation of denatured proteins under stress[1][4][7]. It is highly inducible upon heat shock and cellular stress, but also present at constitutive levels in many tissues[7]. Hsp110 is cytoprotective, promoting cell survival under adverse conditions, and plays roles in immune modulation and protein quality control[3][4]. It is implicated in cancer, neurodegeneration, and infections, where its expression is often elevated and may influence disease progression or therapeutic response[3][5][8]. No small-molecule drugs targeting Hsp110 are approved, but its modulation (e.g., via celastrol) shows therapeutic potential, especially in cancer and neuroprotection[4]. Safety concerns focus on the risk of disrupting essential cellular stress and folding pathways, with possible toxicities if systemically inhibited[8].

Other names

Hsp105HSPH1SSEHeat shock protein 110 kDaHeat shock protein family H (Hsp110) member 1

Induction of Hsp110 expression enhances cytoprotection and cellular stress resistance, Potential drug candidates may inhibit chaperone function or modulate immune activity