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

Arrigoni, Giorgio LU ; Pagano, Mario; Sarno, Stefania; Cesaro, Luca; James, Peter LU and Pinna, Lorenzo (2008) In Journal of Proteome Research 7(3). p.990-1000
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
CK2, regulatory subunit, protein kinase, protein-protein interaction, phosphoproteins, mass spectrometry, affinity chromatography
in
Journal of Proteome Research
volume
7
issue
3
pages
990 - 1000
publisher
The American Chemical Society
external identifiers
  • pmid:18220339
  • wos:000253825100014
  • scopus:44449091164
ISSN
1535-3893
DOI
10.1021/pr070500s
language
English
LU publication?
yes
id
da45e4ad-7001-43fb-8927-b9afea392af0 (old id 1021105)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18220339?dopt=Abstract
date added to LUP
2008-02-19 13:35:01
date last changed
2017-04-09 03:46:10
@article{da45e4ad-7001-43fb-8927-b9afea392af0,
  abstract     = {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.},
  author       = {Arrigoni, Giorgio and Pagano, Mario and Sarno, Stefania and Cesaro, Luca and James, Peter and Pinna, Lorenzo},
  issn         = {1535-3893},
  keyword      = {CK2,regulatory subunit,protein kinase,protein-protein interaction,phosphoproteins,mass spectrometry,affinity chromatography},
  language     = {eng},
  number       = {3},
  pages        = {990--1000},
  publisher    = {The American Chemical Society},
  series       = {Journal of Proteome Research},
  title        = {Mass Spectrometry Analysis of a Protein Kinase CK2 beta Subunit Interactome Isolated from Mouse Brain by Affinity Chromatography.},
  url          = {http://dx.doi.org/10.1021/pr070500s},
  volume       = {7},
  year         = {2008},
}