Molecular mechanisms directing PRC2 recruitment and H3K27 methylation Journal Article


Authors: Laugesen, A.; Højfeldt, J. W.; Helin, K.
Article Title: Molecular mechanisms directing PRC2 recruitment and H3K27 methylation
Abstract: The polycomb repressive complex 2 (PRC2) is a chromatin-associated methyltransferase catalyzing mono-, di-, and trimethylation of lysine 27 on histone H3 (H3K27). This activity is required for normal organismal development and maintenance of gene expression patterns to uphold cell identity. PRC2 function is often deregulated in disease and is a promising candidate for therapeutic targeting in cancer. In this review, we discuss the molecular mechanisms proposed to take part in modulating PRC2 recruitment and shaping H3K27 methylation patterns across the genome. This includes consideration of factors influencing PRC2 residence time on chromatin and PRC2 catalytic activity with a focus on the mechanisms giving rise to regional preferences and differential deposition of H3K27 methylation. We further discuss existing evidence for functional diversity between distinct subsets of PRC2 complexes with the aim of extracting key concepts and highlighting major open questions toward a more complete understanding of PRC2 function. PRC2 function is crucial for the specification and maintenance of cellular identity during normal development and is often deregulated in disease. Laugesen et al. discuss the orchestration of PRC2 recruitment and deposition of H3K27 methylation by factors influencing PRC2 residence time at specific chromatin regions and modulating its catalytic activity. © 2019 Elsevier Inc.
Keywords: unclassified drug; review; binding affinity; gene expression; protein; enzyme activity; genome analysis; amino terminal sequence; epigenetics; chromatin; histone h3; transcription; catalysis; molecular biology; dna binding; polycomb group protein; histone modification; biodiversity; histone methylation; ezh2; polycomb; suz12 protein; prc2; polycomb repressive complex 2; cancer; human; h3k27; lysine 27 on histone h3; retention time
Journal Title: Molecular Cell
Volume: 74
Issue: 1
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2019-04-04
Start Page: 8
End Page: 18
Language: English
DOI: 10.1016/j.molcel.2019.03.011
PUBMED: 30951652
PROVIDER: scopus
PMCID: PMC6452890
DOI/URL:
Notes: Review -- Export Date: 1 May 2019 -- Source: Scopus
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MSK Authors
  1. Kristian Helin
    3 Helin