The BioGRID | PUBLICATION VIEW

	FEBS Lett. Sep (2001); 505(1):42-6
The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.
Roher N, Sarno S, Miro F, Ruzzene M, Llorens F, Meggio F, Itarte E, Pinna LA, Plana M
Department de Bioquimica i Biologia Molcular, Facultat de Ciencies, Universitat Autonoma de Barcelona, Spain.
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 (CK2 alpha) under non-stressed conditions. A K(D) of 4 x 10(-7) was determined for this binding. Heparin competed with Grp94-CT for binding to CK2 alpha. CK2 beta also inhibited the binding of Grp94-CT to CK2 alpha, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2 alpha mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74-77) present in helix C of CK2 alpha. Grp94-CT stimulated the activity of CK2 alpha wild-type but was ineffective on the CK2 alpha K74-77A mutant.
[PUBMED: 11557039]