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The carboxy‐terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme
Author(s) -
Roher Nerea,
Sarno Stefania,
Miró Francesc,
Ruzzene Maria,
Llorens Franc,
Meggio Flavio,
Itarte Emilio,
Pinna Lorenzo A,
Plana Maria
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02781-8
Subject(s) - protein subunit , biochemistry , mutant , chemistry , binding site , surface plasmon resonance , casein kinase 2 , kinase , protein kinase a , mitogen activated protein kinase kinase , gene , materials science , nanoparticle , nanotechnology
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 K D 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.