Lysine acetylation: codified crosstalk with other posttranslational modifications

By Xiang-Jiao Yang, E. Seto. Molecules and Cells, 2008

1,010 citations recorded by the source corpus.

Lysine acetylation has emerged as a major posttranslational modification for histones. Cross-regulation between this and other modifications is crucial in modulating chromatin-based transcriptional control and shaping inheritable epigenetic programs. In addition to histones, many other nuclear proteins and various cytoplasmic regulators are subject to lysine acetylation. This review focuses on recent findings pertinent to acetylation of non-histone proteins and emphasizes how this modification might crosstalk with phosphorylation, methylation, ubiquitination, sumoylation, proline isomerization, and others to form code-like multisite modification programs for dynamic control of cellular signaling under diverse conditions.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/720bcfd749e3172cf71aa8f532c13751ae678523

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Citations in the corpus

Erasers of histone acetylation: the histone deacetylase enzymes. (2014, background): “Cross-regulatory events between acetylation/deacetylation and other posttranslation modifications even extend to nonhistones (reviewed by Yang and Seto 2008).”
A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles (2011, background): “cluding acetylation, methylation, and SUMOylation (52).”
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse (2011, background): “Although PTMs from 18 organisms are included in PSP, 99.7% are mammalian.”
Histone Deacetylase Inhibitors as Anticancer Drugs (2017, background): “Most of the classic HDACs form large complexes with multiple transcriptional co-repressors (such as Sin3 (Transcriptional regulatory protein SIN3), NuRD (Nucleosome remodeling and deacetylase complex), NcoR (Nuclear receptor co-repressor) and SMRT (Silencing mediator of retinoic acid and thyroid hor”
Post-translational modifications in proteins: resources, tools and prediction methods (2021, background): “remove an acetyl group on lysine side chains (Figure 3B) (54).”