The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme

Nerea Roher, Stefania Sarno, Francesc Miró, Maria Ruzzene, Franc Llorens, Flavio Meggio, Emilio Itarte, Lorenzo A. Pinna, Maria Plana

Research output: Contribution to journalArticleResearchpeer-review

11 Citations (Scopus)

Abstract

Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518-803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A KD of 4×10-7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74-77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74-77A mutant. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)42-46
JournalFEBS Letters
Volume505
DOIs
Publication statusPublished - 7 Sep 2001

Keywords

  • Grp94
  • Molecular chaperone
  • Protein kinase CK2
  • Surface plasmon resonance

Fingerprint Dive into the research topics of 'The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme'. Together they form a unique fingerprint.

  • Cite this