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Mass Spectrometry Analysis of a Protein Kinase CK2 beta Subunit Interactome Isolated from Mouse Brain by Affinity Chromatography.

  • Giorgio Arrigoni
  • Mario Pagano
  • Stefania Sarno
  • Luca Cesaro
  • Peter James
  • Lorenzo Pinna
Publishing year: 2008
Language: English
Pages: 990-1000
Publication/Series: Journal of Proteome Research
Volume: 7
Issue: 3
Document type: Journal article
Publisher: The American Chemical Society

Abstract english

CK2, an acronym derived from the misnomer "casein kinase 2", denotes a ubiquitous and extremely pleiotropic Ser/Thr protein kinase, the holoenzyme of which is composed of two catalytic (alpha and/or alpha') and two noncatalytic beta subunits acting as a docking platform and the multifarious functions of which are still incompletely understood. By combining affinity chromatography and mass spectrometry, we have identified 144 mouse brain proteins that associate with immobilized CK2beta. A large proportion (60%) of the identified proteins had been previously reported to be functionally related to CK2, and a similar proportion have been classified as phosphoproteins with approximately half of these having the features of CK2 targets. A large number of the identified proteins ( approximately 40%) either are nuclear or shuttle between the nucleus and cytoplasm, and the biggest functional classes of CK2beta interactors are committed to protein synthesis and degradation (32 proteins) and RNA/DNA interaction (20 proteins). Also well represented are the categories of cytoskeletal/structural proteins (19), trafficking proteins (17), and signaling proteins (14). The identified proteins are examined in relation to their functions and potential as targets and/or regulators of CK2, disclosing in some cases unanticipated links between this kinase and a variety of biochemical events.


  • Immunology in the medical area
  • CK2
  • regulatory subunit
  • protein kinase
  • protein-protein interaction
  • phosphoproteins
  • mass spectrometry
  • affinity chromatography


  • ISSN: 1535-3893
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se


Department of Immunotechnology

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