title: Hsp90@chromatin.nucleus: an emerging hub of a networker.
abstract: The molecular chaperone heat-shock protein of 90 kDa (Hsp90) stabilizes various proteins and occupies a central position in cellular networks. Hsp90 inhibitors are being tested in clinical trials as anticancer drugs. Recent studies have illuminated the unappreciated significance of this chaperone in chromatin transactions and this review focuses on its role in gene expression. By comparing the different mechanisms by which Hsp90 orchestrates transcriptional regulation, the review outlines the contributions of this function to the cellular and organismal phenotype. We chart exciting avenues for research to gain comprehensive insights in the chaperone's importance in cellular physiology, thereby presenting novel opportunities for therapeutic intervention.
authors.affiliation: Department of Biosystems Science and Engineering, ETH Zürich, Mattenstrasse 26, 4058 Basel, Switzerland.
authors.forename: Ritwick
authors.initials: R
authors.lastname: Sawarkar
authors.forename: Renato
authors.initials: R
authors.lastname: Paro
mesh_terms: D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D019143:Evolution, Molecular; D005786:Gene Expression Regulation; D053263:Gene Regulatory Networks; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D018869:Heat-Shock Response / Q000235:genetics; D006801:Humans
chemical_list: D002843:Chromatin; D018841:HSP90 Heat-Shock Proteins