PubMed: 22033876

Title
Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.
Journal
Acta neuropathologica
Volume
123
Issue
None
Pages
105-17
Date
2012-01-01
Authors
Davies P | Funk KE | Kuret J | Liao Z | Thomas SN | Wan Y | Yang AJ

Evidence 4821d748af

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254.

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