Dissection of the dual function of the β‐subunit of protein kinase CK2 (‘casein kinase‐2’): a synthetic peptide reproducing the carboxyl‐terminal domain mimicks the positive but not the negative effects of the whole protein

FEBS Letters

Issinger, Olaf-G.²  Boldyreff, Brigitte²  Pinna, Lorenzo A.¹  Marin, Oriano¹  Meggio, Flavio¹ 

[1] Dipartimento di Chimica Biologica, CRIBI and CNR, Centro per lo Studio della Fisiologia Mitocondriale, Università di Padova, via Trieste 75, 35121 Padova, Italy;Institut für Humangenetik, Universität des Saarlandes, D-66421 Homburg, Germany

关键词: Protein kinase CK2;    Casein kinase-2;    Protein phosphorylation;    Calmodulin phosphorylation;    CK2 β-subunit;   

DOI  :  10.1016/0014-5793(95)00295-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dual function of the regulatory β-subunit of protein kinase CK2 is highlighted by its ability to abolish calmodulin phosphorylation in contrast to its stimulatory effect on the phosphorylation of peptide substrates. Here we show that a synthetic peptide reproducing the C-terminal region of the β-subunit (β[170–215]) stimulates to a similar extent the phosphorylation of either the peptide substrate or calmodulin and also protects the catalytic α-subunit against thermal inactivation as efficiently as full-length β-subunit. These data show that the positive and negative functions of the β-subunit reside in physically separated domains and that the elements responsible for positive regulation are located in the C-terminal region.

【 授权许可】

Unknown