Detection of Post-translationally Modified p53 by Western Blotting

Anna Estevan Barber, David W. Meek (Lead / Corresponding author)

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

Abstract

The p53 tumor suppressor has a central role in many key cellular processes including the DNA damage response, aging, stem cell differentiation, and fertility. p53 undergoes extensive regulatory post-translational modification through events such as phosphorylation, acetylation, methylation, and ubiquitylation. Here, we describe western blotting-based methodology for the detection and relative quantification of individual phosphorylation events in p53. While we focus on well-established N-terminal modifications for the purpose of illustration, this approach can be used to investigate other post-translational modifications of the protein, drawing upon a broad range of commercially available modification-specific antibodies.

Original languageEnglish
Title of host publicationCell Cycle Checkpoints
Subtitle of host publicationMethods and Protocols
EditorsJames J. Manfredi
Place of PublicationNew York
PublisherHumana Press
Pages7-18
Number of pages12
Edition1
ISBN (Electronic)9781071612170
ISBN (Print)9781071612163 (hbk), 9781071612194 (pbk)
DOIs
Publication statusPublished - 2021

Publication series

NameMethods in Molecular Biology
Volume2267
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • DNA-damage response
  • Phospho-specific antibodies
  • Phosphorylation
  • Post-translational modifications
  • Western blot
  • p53

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