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Cohen TJ, Guo JL, Hurtado DE, Kwong LK, Mills IP, Trojanowski JQ, Lee VM. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun. 2011;2:252. PubMed.
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Comments
Universidad Autónoma de Madrid
From a single human gene, many different forms of tau protein could arise. Some of these forms come from alternative splicing of the nuclear RNA transcript, but other forms are the consequence of a post-translational modification—phosphorylation. Recently, an additional modification for tau protein has been indicated—acetylation (Min et al., 2010).
In the last issue of Nature Communications, the group of Virginia Lee has observed that tau acetylation takes place in a key residue, lysine 280, which plays a role in the interaction of tau with microtubules. This finding shows how acetylation could regulate one of the main tau functions—its interaction with microtubules—but the report also opens the door for future experiments. Cohen et al. reported that tau deacetylation could occur through histone deacetylase 6 (HDA6), a deacetylase that is inhibited by tau. This hints that tau protein could self-regulate its deacetylation. This could be tested in the future. Secondly, it remains to be determined if acetylated tau could be deacetylated by more than one deacetylase. Lastly, as indicated in this paper, tau-lysine 280 is present in a motif that is similar to those present in other microtubule-associated proteins like MAP2 or MAP4. Thus, acetylation could be a common mechanism to regulate the interaction of some MAPs with microtubules, as the authors have proposed.
In summary, this is an interesting and seminal work on the regulation of tau function.
References:
Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, Huang EJ, Shen Y, Masliah E, Mukherjee C, Meyers D, Cole PA, Ott M, Gan L. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron. 2010 Sep 23;67(6):953-66. PubMed.
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