Mixed lineage leukemia: a structure-function perspective of the MLL1 protein

被引：87

作者：

Cosgrove, Michael S. ^{[1
]}

Patel, Anamika ^{[1
]}

机构：

[1] Syracuse Univ, Dept Biol, Syracuse, NY 13244 USA

来源：

FEBS JOURNAL | 2010年 / 277卷 / 08期

关键词：

Ash2L; CXXC; H3K4; methylation; MLL; RbBP5; SET; TAD; WDR5; Win motif; HISTONE LYSINE METHYLTRANSFERASES; TRANSCRIPTION FACTOR-BINDING; ONCOPROTEIN MLL; MOLECULAR RECOGNITION; PRODUCT SPECIFICITY; H3K4; TRIMETHYLATION; PHE/TYR SWITCH; CORE COMPLEX; SET DOMAINS; KIX DOMAIN;

D O I：

10.1111/j.1742-4658.2010.07609.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several acute lymphoblastic and myelogenous leukemias are correlated with alterations in the human mixed lineage leukemia protein-1 (MLL1) gene. MLL1 is a member of the evolutionarily conserved SET1 family of histone H3 lysine 4 (H3K4) methyltransferases, which are required for the regulation of distinct groups of developmentally regulated genes in metazoans. Despite the important biological role of SET1 family enzymes and their involvement in human leukemias, relatively little is understood about how these enzymes work. Here we review several recent structural and biochemical studies that are beginning to shed light on the molecular mechanisms for the regulation of H3K4 methylation by the human MLL1 enzyme.

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页码：1832 / 1842

页数：11

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