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Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Induction and activation of the p53 pathway: a role for the protein kinase CK2?

David W Meek1, Miranda Cox

  • 1Biomedical Research Institute, Ninewells Hospital, University of Dundee, Dundee DD1 9SY, UK. d.w.meek@dundee.ac.uk

Molecular and Cellular Biochemistry
|July 20, 2011
PubMed

Insights

Protein kinase CK2

Area of Science:

  • Cellular Biology
  • Molecular Oncology
  • Biochemistry

Background:

  • Protein kinase CK2 is implicated in numerous cellular processes and diseases, including cancer.
  • CK2 is known to phosphorylate many proteins in vitro, but its physiological substrates and roles are still being elucidated.
  • The tumor suppressor protein p53 is a known in vitro substrate of CK2, but its in vivo interaction requires further investigation.

Purpose of the Study:

  • To investigate the physiological relevance of protein kinase CK2 (CK2) phosphorylating the tumor suppressor protein p53.
  • To elucidate the mechanism regulating p53 phosphorylation at Ser392 by CK2.
  • To assess the in vivo significance of the CK2-p53 interaction in cellular surveillance.

Main Methods:

  • Analysis of p53 phosphorylation at Ser392.
  • Investigation of the relationship between p53 protein turnover rate and phosphorylation stoichiometry.
  • Comparison of in vitro and in vivo phosphorylation events.
  • Examination of CK2 activity in cell extracts.

Main Results:

  • Phosphorylation of p53 at Ser392 by CK2 is regulated by p53 protein turnover rate.
  • CK2 is the sole detectable Ser392 protein kinase in cell extracts.
  • Data suggest uncertainty regarding the in vivo physiological relevance of CK2-mediated p53 Ser392 phosphorylation.

Conclusions:

  • The stoichiometry of p53 Ser392 phosphorylation by CK2 is governed by p53 protein turnover.
  • While CK2 phosphorylates p53 in vitro and is present in cell extracts, its in vivo role in p53 Ser392 phosphorylation requires further experimental validation.
  • Further research is needed to clarify the relationship between CK2 and the p53 anti-cancer surveillance system.

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