title: YEATS Domain-A Histone Acylation Reader in Health and Disease.
abstract: Histone post-translational modifications (PTMs) carry an epigenetic layer of message to regulate diverse cellular processes at the chromatin level. Many of these PTMs are selectively recognized by dedicated effector proteins for normal cell growth and development, while dysregulation of these recognition events is often implicated in human diseases, notably cancer. Thus, it is fundamentally important to elucidate the regulatory mechanism(s) underlying the readout of PTMs on histones. The Yaf9, ENL, AF9, Taf14, Sas5 (YEATS) domain is an emerging reader module that selectively recognizes histone lysine acylation with a preference for crotonylation over acetylation. In the review, we discuss the recognition of histone acylations by the YEATS domain and the biological significance of this readout from multiple perspectives.
authors.affiliation: MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, P.R. China; Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, P.R. China.
authors.forename: Dan
authors.initials: D
authors.lastname: Zhao
authors.affiliation: MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, P.R. China; Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, P.R. China.
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Li
authors.affiliation: MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, P.R. China; Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, P.R. China.
authors.forename: Xiaozhe
authors.initials: X
authors.lastname: Xiong
authors.affiliation: MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, P.R. China; Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, P.R. China.
authors.forename: Zhonglei
authors.initials: Z
authors.lastname: Chen
authors.affiliation: MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, P.R. China; Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, P.R. China. Electronic address: lht@tsinghua.edu.cn.
authors.forename: Haitao
authors.initials: H
authors.lastname: Li
mesh_terms: D000215:Acylation; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D005786:Gene Expression Regulation; D006657:Histones / Q000378:metabolism*; D006801:Humans; D009369:Neoplasms / Q000503:physiopathology*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D006657:Histones
keywords: YEATS domain; aromatic-π stacking; epigenetic regulation; histone acylation; lysine crotonylation