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Frontiers in Biology

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ISSN 1674-7992(Online)

CN 11-5892/Q

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Front. Biol.    2016, Vol. 11 Issue (1) : 10-18    https://doi.org/10.1007/s11515-016-1390-6
REVIEW
Cellular functions of MLL/SET-family histone H3 lysine 4 methyltransferase components
J. K. Bailey1,2,Dzwokai Ma1,2,*()
1. Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106, USA
2. Neuroscience Research Institute, University of California, Santa Barbara, CA 93106, USA
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Abstract

The MLL/SET family of histone H3 lysine 4 methyltransferases form enzyme complexes with core subunits ASH2L, WDR5, RbBP5, and DPY-30 (often abbreviated WRAD), and are responsible for global histone H3 lysine 4 methylation, a hallmark of actively transcribed chromatin in mammalian cells. Accordingly, the function of these proteins is required for a wide variety of processes including stem cell differentiation, cell growth and division, body segmentation, and hematopoiesis. While most work on MLL-WRAD has focused on the function this core complex in histone methylation, recent studies indicate that MLL-WRAD proteins interact with a variety of other proteins and lncRNAs and can localize to cellular organelles beyond the nucleus. In this review, we focus on the recently described activities and interacting partners of MLL-WRAD both inside and outside the nucleus.
Keywords H3K4MT      histone H3 lysine 4 methyltransferase      WDR5      RbBP5      ASH2L      DPY-30      SET      MLL      WRAD      Oct4      MYC      cell biology      protein lysine methylation     
Corresponding Author(s): Dzwokai Ma   
Just Accepted Date: 22 February 2016   Online First Date: 16 March 2016    Issue Date: 22 March 2016
 Cite this article:   
J. K. Bailey,Dzwokai Ma. Cellular functions of MLL/SET-family histone H3 lysine 4 methyltransferase components[J]. Front. Biol., 2016, 11(1): 10-18.
 URL:  
https://academic.hep.com.cn/fib/EN/10.1007/s11515-016-1390-6
https://academic.hep.com.cn/fib/EN/Y2016/V11/I1/10
Fig.1  Summary of MLL-WRAD functions and interactions within cells. Methylation of histone H3 at lysine 4 (K4) within the nucleus is the most thoroughly studied function of the MLL-WRAD complex. However, recent findings indicate that WDR5 works in concert with transcription factors including MYC, C/EBPα, and Oct4 to read/write epigenetic marks in gene-specific contexts. WDR5 also interacts with other chromatin-related factors such as KANSL1, KANSL2, the multifunctional influenza virus protein NS1, and many long noncoding RNAs (only NeST and HOTTIP are depicted). Cytoplasmic localization of MLL-WRAD proteins has also been reported at mitochondria during viral infection (with TRAF3, TRAF6, and VISA), at the Golgi and trans-Golgi network (with BIG1 and PAQR3), and at the midbody during the final stages of cell division (with PRC1, MKLP1, and CYK4). Although in many cases only a single MLL-WRAD component was investigated, other subunits may work together to facilitate downstream events. Dotted lines indicate interactions that may be direct or indirect.
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