HDAC6 is a microtubule-associated deacetylase
By Charlotte C. Hubbert, Amaris R. Guardiola, R. Shao, Y. Kawaguchi, A. Ito, Andrew Nixon, Minoru Yoshida, Xiao-Fan Wang, T. Yao. Nature, 2002
2,342 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/fd2bc301cff0a3a5176552b4e6bd638cc3634846
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
- E. Seto
- Xiang-Jiao Yang
- PA Marks
- E. Verdin
- Minoru Yoshida
- Weisheng Xu
- R. Parmigiani
- John Q. Trojanowski
In Oncology
Citations in the corpus
- HEF1-dependent Aurora A activation induces disassembly of the primary cilium. (2007, neutral): “stabilized microtubules prepared from purified bovine brain tubulin (Cytoskeleton) to measure deacetylase activity (as in (Hubbert et al., 2002)) and with -(32)P-ATP (Perkin-Elmer) in AurA”
- New and emerging HDAC inhibitors for cancer treatment. (2014, neutral): “HDAC6 is responsible for α-tubulin deacetylation (90), thus providing a sensitive biomarker for rocilinostat activity during clinical trials.”
- Sirtuins: critical regulators at the crossroads between cancer and aging (2007, background): “Of the sirtuins, only SIRT2 deacetylates tubulin, also a target of the class II deacetylase HDAC6 (Hubbert et al., 2002; Matsuyama et al., 2002; North et al., 2003).”
- HDAC family: What are the cancer relevant targets? (2009, background): “HDAC6 has emerged as a major cytoplasmic deacetylase functioning as ana-tubulin deacetylase [17] and HSP90 deacetylase [18] thereby regulating cell motility, adhesion and chaperone function.”
- HDAC6 modulates cell motility by altering the acetylation level of cortactin. (2007, background): “…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; Matsuyama et al., 2002; Zhang et al., 2003).”
- Post-translational modifications regulate microtubule function (2003, neutral): “By contrast, two enzymes that catalyse the opposing reaction — that is, deacetylation — have been recently describe”
- Off-target toxicity is a common mechanism of action of cancer drugs undergoing clinical trials (2019, background): “For instance, HDAC6 is capable of deacetylating microtubules (26), and HDAC6 inhibition has been reported to render cells vulnerable to drugs that interfere with microtubule dynamics (27).”
- Acetylation of tau inhibits its degradation and contributes to tauopathy. (2010, neutral): “Although expressed at lower levels than SIRT1 and SIRT2, HDAC6 eliminated tubulin acetylation (Hubbert et al., 2002), suggesting”