title: Cross-regulation of histone modifications.
abstract: Histones undergo several different post-translational modifications that control a variety of physiological processes. These covalent modifications show substantial cross-regulation, providing a wealth of regulatory potential. New insights into the communication between modifications on histones have emerged in recent years. This review assesses the current understanding of cross-regulation of histone modifications and identifies future questions to be addressed in this field.
authors.affiliation: Program in Genes and Development, Department of Biochemistry and Molecular Biology and Center for Epigenetics, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
authors.forename: John A
authors.initials: JA
authors.lastname: Latham
authors.forename: Sharon Y R
authors.initials: SY
authors.lastname: Dent
mesh_terms: D000595:Amino Acid Sequence; D042421:Histone Code; D006657:Histones / Q000378:metabolism* / Q000502:physiology; D013058:Mass Spectrometry; D008938:Mitosis / Q000235:genetics; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism
chemical_list: D006657:Histones; D016159:Tumor Suppressor Protein p53