Diverse functions of PHD fingers of the MLL/KMT2 subfamily.

TitleDiverse functions of PHD fingers of the MLL/KMT2 subfamily.
Publication TypeJournal Article
Year of Publication2014
AuthorsAli M, Hom RA, Blakeslee W, Ikenouye L, Kutateladze TG
JournalBiochim Biophys Acta
Volume1843
Issue2
Pagination366-71
Date Published2014 Feb
ISSN0006-3002
KeywordsAmino Acid Sequence, Conserved Sequence, DNA-Binding Proteins, Histones, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary
Abstract

Five members of the KMT2 family of lysine methyltransferases, originally named the mixed lineage leukemia (MLL1-5) proteins, regulate gene expression during embryogenesis and development. Each KMT2A-E contains a catalytic SET domain that methylates lysine 4 of histone H3, and one or several PHD fingers. Over the past few years a growing number of studies have uncovered diverse biological roles of the KMT2A-E PHD fingers, implicating them in binding to methylated histones and other nuclear proteins, and in mediating the E3 ligase activity and dimerization. Mutations in the PHD fingers or deletion of these modules are linked to human diseases including cancer and Kabuki syndrome. In this work, we summarize recently identified biological functions of the KMT2A-E PHD fingers, discuss mechanisms of their action, and examine preference of these domains for histone and non-histone ligands.

DOI10.1016/j.bbamcr.2013.11.016
Alternate JournalBiochim. Biophys. Acta
Citation Key1419
PubMed ID24291127