Histone PTM Crosstalk Stimulates Dot1 Methyltransferase Activity.

Authors :: Cutler JA
Perner F
Armstrong SA
Source :: Trends in biochemical sciences [Trends Biochem Sci] 2021 Jul; Vol. 46 (7), pp. 522-524. Date of Electronic Publication: 2021 Apr 17.
Publication Year :: 2021
Abstract: Valencia-Sánchez et al. have demonstrated that two histone post-translational modifications (PTMs) - H4K16 acetylation (H4K16ac) and H2BK120 ubiquitination (H2Bub) - enhance the methylation of H3K79 (H3K79me) by Dot1. This breakthrough indicates crosstalk between H4Kac/H2Bub/H3K79me and may improve our understanding of the role that Dot1/Dot1L plays in developmental processes and disease, including MLL1/KMT2A(MLL-r) leukemia.<br />Competing Interests: Declaration of Interests S.A.A. has been a consultant and/or shareholder for Neomorph Inc, Imago BioSciences, Vitae/Allergan Pharma, Cyteir Therapeutics, C4 Therapeutics, Accent Therapeutics, and Mana Therapeutics. S.A.A. has received research support from Janssen, Novartis, and Syndax. J.A.C. and F.P. have no conflicts of interest to declare.<br /> (Copyright © 2021. Published by Elsevier Ltd.)