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

doi:https://doi.org/10.1016/S0014-5793(01)02781-8

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

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-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 language	English
Pages (from-to)	42-46
Journal	FEBS Letters
Volume	505
DOIs	https://doi.org/10.1016/S0014-5793(01)02781-8
Publication status	Published - 7 Sep 2001

Keywords

Grp94
Molecular chaperone
Protein kinase CK2
Surface plasmon resonance

Access to Document

https://doi.org/10.1016/S0014-5793(01)02781-8

Cite this

@article{97a07ddf2ed9456883ec1c728454782b,

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

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. {\textcopyright} 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.",

keywords = "Grp94, Molecular chaperone, Protein kinase CK2, Surface plasmon resonance",

author = "Nerea Roher and Stefania Sarno and Francesc Mir{\'o} and Maria Ruzzene and Franc Llorens and Flavio Meggio and Emilio Itarte and Pinna, {Lorenzo A.} and Maria Plana",

year = "2001",

month = sep,

day = "7",

doi = "https://doi.org/10.1016/S0014-5793(01)02781-8",

language = "English",

volume = "505",

pages = "42--46",

}

The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme. / Roher, Nerea; Sarno, Stefania; Miró, Francesc; Ruzzene, Maria; Llorens, Franc; Meggio, Flavio; Itarte, Emilio; Pinna, Lorenzo A.; Plana, Maria.

In: FEBS Letters, Vol. 505, 07.09.2001, p. 42-46.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - The carboxy-terminal domain of Grp94 binds to protein kinase CK2α but not to CK2 holoenzyme

AU - Roher, Nerea

AU - Sarno, Stefania

AU - Miró, Francesc

AU - Ruzzene, Maria

AU - Llorens, Franc

AU - Meggio, Flavio

AU - Itarte, Emilio

AU - Pinna, Lorenzo A.

AU - Plana, Maria

PY - 2001/9/7

Y1 - 2001/9/7

N2 - 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.

AB - 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.

KW - Grp94

KW - Molecular chaperone

KW - Protein kinase CK2

KW - Surface plasmon resonance

U2 - https://doi.org/10.1016/S0014-5793(01)02781-8

DO - https://doi.org/10.1016/S0014-5793(01)02781-8

M3 - Article

VL - 505

SP - 42

EP - 46

ER -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this