Current understanding and importance of histone phosphorylation in regulating chromatin biology.

  • Pérez-Cadahía B
  • Drobic B
  • Khan P
 et al. 
  • 14


    Mendeley users who have this article in their library.
  • 14


    Citations of this article.


The core histones H2A, H2B, H3 and H4, undergo various post-translational modifications, such as acetylation, methylation and phosphorylation. Core histone phosphorylation has roles in several biological responses, including transcription, mitosis, DNA repair and apoptosis. Histone phosphorylation may disrupt chromatin structure and/or provide a 'code' for the recruitment or occlusion of non-histone chromosomal proteins to chromatin. Among the better-characterized histone phosphorylation events are the phosphorylation of H3 at Ser10 and Ser 28, and the phosphorylation of the H2A variant H2A.X at Ser139. Much remains to be learned about the function of the many other core histone phosphorylation events in chromatin. This review provides an overview of the biological roles of core histone phosphorylation in mammalian cells.

Author-supplied keywords

  • Animals
  • Cell Line
  • Chromatin
  • Chromatin: metabolism
  • Chromatin: physiology
  • Histones
  • Histones: metabolism
  • Histones: physiology
  • Humans
  • Mitosis
  • Mitosis: physiology
  • Phosphorylation
  • Protein Processing, Post-Translational

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Beatriz Pérez-Cadahía

  • Bojan Drobic

  • Protiti Khan

  • Chaitra C Shivashankar

  • James R Davie

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free