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Background
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HDAC6 (histone deacetylase 6) is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. HDAC6 plays a central role in microtubule-dependent cell motility via deacetylation of tubulin, and has been shown to interact with HDAC11, SIRT2, and F-actin. HDAC6 is ubiquitinated, but its polyubiquitination however does not lead to degradation. HDAC is also a potential target of sumoylation.
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Background
References
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- Hook, S.S., et al., Proc. Natl. Acad. Sci. U.S.A. 99(21):13425-13430 (2002).
- Grozinger, C.M., et al., Proc. Natl. Acad. Sci. U.S.A. 96(9):4868-4873 (1999).
- Wolffe, A.P., Nature 387(6628):16-17 (1997).
- Pazin, M.J., et al., Cell 89(3):325-328 (1997).
- Mahlknecht, U., et al., Cytogenet. Cell Genet. 93 (1-2), 135-136 (2001).
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