Cross talk between protein kinase CK2 and eukaryotic translation initiation factor eIF2β subunit

Franc Llorens, Stefania Sarno, Eduard Sarró, Anna Duarri, Nerea Roher, Flavio Meggio, Maria Plana, Lorenzo A. Pinna, Emilio Itarte

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

The β-subunit of eukaryotic translation initiation factor eIF2 is a substrate and a partner for protein kinase CK2. Surface plasmon resonance analysis shows that the truncated form corresponding to residues 138-333 of eIF2β (eIF2β-CT) interacts with CK2α as efficiently as full length eIF2β, whereas the form corresponding to residues 1-137, which contains the CK2 phosphorylation sites, (eIF2β-NT) does not bind. The use of different mutants and truncated forms of CK2α allowed us to map the basic segment K74-K83 at the beginning of helix αC and residues R191R195K198 in the p+1 loop as the main determinants for the binding to eIF2β-CT of either the isolated CK2α subunit or the CK2 holoenzyme. The presence of eIF2β-CT stimulated the activity of CK2α towards the RRRAADSDDDDD peptide substrate; effect that was not observed with the CK2α K74-77A whose ability to bind to eIF2β-CT is severely impaired. Gel filtration analysis confirmed the ability of CK2α to form complexes with eIFα-CT, and the contribution of the basic cluster in CK2α (K74-K77) in this association. © Springer Science + Business Media, Inc. 2005.
Original languageEnglish
Pages (from-to)53-61
JournalMolecular and Cellular Biochemistry
Volume274
DOIs
Publication statusPublished - 1 Jun 2005

Keywords

  • Enzymic regulation
  • Protein kinase CK2
  • Protein phosphorylation
  • Protein-protein interaction
  • Surface plasmon resonance
  • eIF2

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