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

https://doi.org/10.1016/j.bbamcr.2013.11.016Get rights and content
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Highlights

  • Biological activities of the PHD fingers of the MLL/KMT2 subfamily are compared.

  • The mechanisms underlying functions of the KMT2A-E PHD fingers are discussed.

  • The conservation of the KMT2A-E PHD-histone interactions is explored.

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.

Keywords

PHD finger
KMT2
MLL
Methyltransferase
Histone
Chromatin

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