Dissection of the dual function of the beta-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.

Abstract:

:The dual function of the regulatory beta-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 beta-subunit (beta[170-215]) stimulates to a similar extent the phosphorylation of either the peptide substrate or calmodulin and also protects the catalytic alpha-subunit against thermal inactivation as efficiently as full-length beta-subunit. These data show that the positive and negative functions of the beta-subunit reside in physically separated domains and that the elements responsible for positive regulation are located in the C-terminal region.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Marin O,Meggio F,Boldyreff B,Issinger OG,Pinna LA

doi

10.1016/0014-5793(95)00295-k

subject

Has Abstract

pub_date

1995-04-17 00:00:00

pages

111-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00295-K

journal_volume

363

pub_type

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