Your browser doesn't support javascript.
loading
YEATS Domain-A Histone Acylation Reader in Health and Disease.
Zhao, Dan; Li, Yuanyuan; Xiong, Xiaozhe; Chen, Zhonglei; Li, Haitao.
Afiliação
  • Zhao D; 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. Chin
  • Li Y; 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. Chin
  • Xiong X; 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. Chin
  • Chen Z; 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. Chin
  • Li H; 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. Chin
J Mol Biol ; 429(13): 1994-2002, 2017 06 30.
Article em En | MEDLINE | ID: mdl-28300602
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.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Cromossômicas não Histona / Histonas / Processamento de Proteína Pós-Traducional / Regulação da Expressão Gênica / Neoplasias Limite: Humans Idioma: En Revista: J Mol Biol Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Cromossômicas não Histona / Histonas / Processamento de Proteína Pós-Traducional / Regulação da Expressão Gênica / Neoplasias Limite: Humans Idioma: En Revista: J Mol Biol Ano de publicação: 2017 Tipo de documento: Article