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.

journal_name

Trends Cell Biol

journal_title

Trends in cell biology

authors

Sawarkar R,Paro R

doi

10.1016/j.tcb.2012.11.007

subject

Has Abstract

pub_date

2013-04-01 00:00:00

pages

193-201

issue

4

eissn

0962-8924

issn

1879-3088

pii

S0962-8924(12)00221-8

journal_volume

23

pub_type

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