HDAC‐6 interacts with and deacetylates tubulin and microtubules in vivo
By Yu Zhang, Na Li, C. Caron, G. Matthias, D. Hess, S. Khochbin, P. Matthias. EMBO Journal, 2003
740 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/19f246c77ac6be3d013a27d8b3cd37908ce01fe2
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Citations in the corpus
- HEF1-dependent Aurora A activation induces disassembly of the primary cilium. (2007, positive): “HDAC6 tightly interacts with and tubulins through its HDAC domain, which may restrict its enzymatic activity, based on reports that taxol treatment causes HDAC6 to accumulate on microtubules, and is accompanied by increased tubulin acetylation (Zhang et al., 2003).”
- 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).”
- The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men (2008, background): “HDAC6 has been shown to function as an α-tubulin deacetylas”
- Therapeutic application of histone deacetylase inhibitors for central nervous system disorders (2008, background): “In addition to modification of histones, other (non-histone) cellular proteins are substrates for HDACs, and these proteins mediate diverse biological functions via transcriptional-dependent as well as independent mechanism”
- Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. (2004, background): “Consistent with this idea, HDAC6 deacetylates the cytoplasmic protein tubulin.(10,58,59) In addition, HDAC10 is reported to associate with HDAC3 and SMRT,(40,60) while HDAC6 apparently lacks these associations and instead associates with the class 4 HDAC11 protein.”
- Post-translational modifications regulate microtubule function (2003, neutral): “By contrast, two enzymes that catalyse the opposing reaction — that is, deacetylation — have been recently describe”