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 Lettjournal_title
FEBS lettersauthors
Marin O,Meggio F,Boldyreff B,Issinger OG,Pinna LAdoi
10.1016/0014-5793(95)00295-ksubject
Has Abstractpub_date
1995-04-17 00:00:00pages
111-4issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(95)00295-Kjournal_volume
363pub_type
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