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. 2019 Dec 19;12(1):21. doi: 10.3390/cancers12010021

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Localization and described functions of HSP110 and HSP70 within the STAT3 and STAT5 signaling pathways. HSP110 directly binds to STAT3 in the cytosol and favors its phosphorylation through JAK2, and, through this mechanism, participates in the promotion of cell proliferation. HSP110α and HSP110β localize to the cytoplasm and nucleus of cells, respectively. HSP110β induces the expression of HSP70 in mammalian cells. Overexpression of HSP110β stimulated the phosphorylation of STAT3 (Tyr705) and its translocation to the nucleus. STAT3 binds to the sequence of the HSP70 promoter at the level of a sequence (−206 to −187 base pair) whose mutation abrogated the activation of the HSP110β-mediated HSP70 promoter. HSP70 directly interacts with STAT3 and STAT5. It favors STAT3 phosphorylation and activity, and STAT5 levels, phosphorylation, and activity.