HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor.

By Jeffrey J Kovacs, P. Murphy, S. Gaillard, Xuan Zhao, June-Tai Wu, C. Nicchitta, Minoru Yoshida, D. Toft, W. Pratt, T. Yao. Molecules and Cells, 2005

1,160 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7d0a2d3611e14a663c7e783e5f0864f06ce0f608

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Ryuji Hamamoto
2. Yusuke Nakamura
3. Makoto Nakakido
4. PA Marks
5. Xiang-Jiao Yang
6. G. Toyokawa
7. E. Seto
8. K. Ueda

Citations in the corpus

• Histone Deacetylase Inhibitors: Overview and Perspectives (2007, background): “Inhibition or knockdown of HDAC6 induces heat shock protein-90 acetylation and inhibits its chaperone activity (21, 22).”
• Post-translational modifications in signal integration (2010, background): “Acetylation also influences protein-protein interactions, as in the case of heat shock protein 90 (HSP90), whose acetylation increases its interaction with its client protein, glucocorticoid recepto”
• SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “293T cells were co-transfected with a FLAGSMYD2 expression vector and four different lengths of HA-HSP90AB1 vectors ([1–724], [1–500], [250–724] and [500–724]).”
• HSP90 at the hub of protein homeostasis: emerging mechanistic insights (2010, background): “Acetylation of Lys294 in the middle domain by an unknown acetylase inhibits both client protein maturation and co-chaperone bindin”
• Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “Later studies revealed that HDAC6 binds Hsp90 and reverses its acetylation (Bali et al., 2005; Kovacs et al., 2005).”
• New and emerging HDAC inhibitors for cancer treatment. (2014, neutral): “Hsp90 becomes dissociated from its client proteins, leading to the ubiquitylation and degradation of immature, misfolded proteins (84).”
• The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men (2008, background): “The heat shock chaperone protein HSP90 also associates with HDAC6 and is a bona fide cytoplasmic substrat”
• HDAC6 modulates cell motility by altering the acetylation level of cortactin. (2007, background): “N IH -PA Author M anuscript N IH -PA Author M anuscript N IH -PA Author M anuscript Discussion Results from previous studies have shown that HDAC6 associates with and regulates the acetylation of α-tubulin and Hsp90 (Bali et al., 2005; Haggarty et al., 2003; Hubbert et al., 2002; Kovacs et al., 2005”
• Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer (2006, background): “HSP90 hyper-acetylation in HDAC6-deficient cells leads to the loss of chaperone activit”
• The NAD+-Dependent Deacetylase SIRT1 Modulates CLOCK-Mediated Chromatin Remodeling and Circadian Control (2008, neutral): “HDACs have also been implicated in the reversible acetylation of nonhistone proteins, including p53 (Luo et al., 2001; Vaziri et al., 2001), Hsp90 ( Kovacs et al., 2005 ), MyoD (Mal et al., 2001), and E2F1 (Martinez-Balbas et al., 2000).”
• Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators. (2006, positive): “Few compounds inhibit HSP90 through mechanisms outside this N-terminal domain (Bali et al., 2005; Kovacs et al., 2005; Marcu et al., 2000).”
• Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “Notably, it has been shown that HDAC6 regulates the activity of the chaperone heat shock protein 90 (HSP90), which provides an additional mechanistic insight into the role of this deacetylase in protein degradatio”
• Energy Metabolism in the Liver (2014, positive): “HDAC6 deacetylates HSP90 and promotes GR-HSP90 complex assembly (123), and deletion of HDAC6 blocks ligand-induced nuclear”