Abstract

Lysine-specific methyltransferase 7 (KMT7) SET7/9, aka Set7, Set9, or SetD7, or KMT5 was discovered 20 years ago, yet its biological role remains rather enigmatic. In this review, we analyze the particularities of SET7/9 enzymatic activity and substrate specificity with respect to its biological importance, mostly focusing on its two well-characterized biological functions: cellular proliferation and stress response.

Highlights

  • Methyltransferases are a compendium of diverse enzymes, most of which use Sadenosyl-methionine (Ado-Met) as a donor of methyl groups

  • The basic methyl group transfer reaction is the catalytic attack of a nucleophile on a methyl group to form methylated derivatives of proteins, lipids, polysaccharides, nucleic acids, and various small molecules

  • Small-molecule inhibitors are promising tools that allow for the probing functions of methyltransferases in diseases

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Summary

Introduction

Methyltransferases are a compendium of diverse enzymes, most of which use Sadenosyl-methionine (Ado-Met) as a donor of methyl groups. The in vitro studies showed that SET7/9 is able to methylate TAF7 at the lysine residue K5 [8], which points to SET7/9 being involved in the TAF7-dependent regulation of its target genes, in response to heat shock [56] (Table 1). YAP1 and TAZ are integral components of the β-catenin destruction complex while the β-catenin/TCF4 complex binds enhancer elements of the YAP gene to drive YAP expression in colorectal cancer cells [58,59] Taken together, these facts indicate that SET7/9 may be considered as one of the key regulators of the Wnt/β-catenin and Hippo signaling pathways. Catenin destruction complex while the β-catenin/TCF4 complex binds enhancer elements of the YAP gene to drive YAP expression in colorectal cancer cells [58,59] Taken together, these facts indicate that SET7/9 may be considered as one of the key regulators o7fotfh1e3 Wnt/β-catenin and Hippo signaling pathways.

SET7/9 and STAATT33
Findings
10. Concluding Remarks
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