Editors' ChoiceDeacetylation

Tubulin Gets Targeted

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Science's STKE  11 Mar 2003:
Vol. 2003, Issue 173, pp. tw98-TW98
DOI: 10.1126/stke.2003.173.tw98

Histone proteins are the best-characterized substrates for acetylation and deacteylation, but the list of nonhistone protein targets continues to grow. For example, acetylation of tubulin has a stabilizing effect. Zhang et al. have now identified a deactylase that acts on tubulin. Histone deacetylase-6 (HDAC-6) interacted with tubulin in a yeast two-hydrid screen. It also partially colocalized with and immunoprecipitated with microtubules in cultured mammalian cells. Purified HDAC-6 deactylated tubulin in vitro. Overexpression of HDAC-6 in mammalian cells caused a decrease in tubulin acetylation, and this effect was blocked by treating cells with pharmacological inhibitors of HDAC-6. Finally, disruption of the HDAC-6 gene in embryonic stem cells resulted in decreased tubulin acetylation. Because histone deacetylation was not affected in these HDAC-6-null cells, nor were there proliferative effects, the authors suggest that the main function of HDAC-6 could be to control the microtubule network rather than chromosome dynamics. In fact, HDAC-6 did not colocalize with DNA during mitosis.

Y. Zhang, N. Li, C. Caron, G. Matthias, D. Hess, S. Khochbin, P. Matthias, HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 22, 1168-1179 (2003). [Abstract] [Full Text]

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