Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome

Stefan Uhle, Ohad Medalia, Richard Waldron, Renate Dumdey, Peter Henklein, Dawadschargal Bech-Otschir, Xiaohua Huang, Matthias Berse, Joseph Sperling, Rüdiger Schade, Wolfgang Dubiel

Research output: Contribution to journalArticlepeer-review

174 Scopus citations


The COP9 signalosome (CSN) purified from human erythrocytes possesses kinase activity that phosphorylates proteins such as c-Jun and p53 with consequence for their ubiquitin (Ub)-dependent degradation. Here we show that protein kinase CK2 (CK2) and protein kinase D (PKD) co-purify with CSN. Immunoprecipitation and far-western blots reveal that CK2 and PKD are in fact associated with CSN. As indicated by electron microscopy with gold-labeled ATP, at least 10% of CSN particles are associated with kinases. Kinase activity, most likely due to CK2 and PKD, co-immunoprecipitates with CSN from HeLa cells. CK2 binds to ΔCSN3(111-403) and CSN7, whereas PKD interacts with full-length CSN3. CK2 phosphorylates CSN2 and CSN7, and PKD modifies CSN7. Both CK2 and PKD phosphorylate c-Jun as well as p53. CK2 phosphorylates Thr155, which targets p53 to degradation by the Ub system. Curcumin, emodin, DRB and resveratrol block CSN-associated kinases and induce degradation of c-Jun in HeLa cells. Curcumin treatment results in elevated amounts of c-Jun-Ub conjugates. We conclude that CK2 and PKD are recruited by CSN in order to regulate Ub conjugate formation.

Original languageEnglish
Pages (from-to)1302-1312
Number of pages11
JournalEMBO Journal
Issue number6
StatePublished - 17 Mar 2003
Externally publishedYes


  • C-Jun
  • COP9 signalosome
  • P53
  • Protein kinase CK2
  • Protein kinase D

ASJC Scopus subject areas

  • Neuroscience (all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology (all)
  • Immunology and Microbiology (all)


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