Histone PTM Crosstalk Stimulates Dot1 Methyltransferase Activity

Jevon A Cutler; Florian Perner; Scott A Armstrong

doi:10.1016/j.tibs.2021.04.001

Histone PTM Crosstalk Stimulates Dot1 Methyltransferase Activity

Trends Biochem Sci. 2021 Jul;46(7):522-524. doi: 10.1016/j.tibs.2021.04.001. Epub 2021 Apr 17.

Authors

Jevon A Cutler¹, Florian Perner², Scott A Armstrong³

Affiliations

¹ Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
² Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Internal Medicine C, Greifswald University Medical Center, Greifswald 17475, Germany.
³ Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Division of Hematology-Oncology, Boston Children's Hospital, Boston, MA 02115, USA. Electronic address: scott_armstrong@dfci.harvard.edu.

PMID: 33879367
DOI: 10.1016/j.tibs.2021.04.001

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.

Keywords: acetylation; leukemia; methylation; therapeutic targeting; ubiquitination.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Comment

MeSH terms

Acetylation
Histones* / metabolism
Methylation
Protein Processing, Post-Translational*
Ubiquitination

Substances

Histones

Abstract

Publication types

MeSH terms

Substances

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