Phosphorylation of type II (beta) protein kinase C by casein kinase II.

Abstract:

:Rat brain type II (beta) protein kinase C (PKC) was phosphorylated by rat lung casein kinase II (CK-II). Neither type I (gamma) nor type III (alpha) PKC was significantly phosphorylated by CK-II. CK-II incorporated 0.2-0.3 mol of phosphate into 1 mol of type II PKC. This phosphate was located at the single seryl residue (Ser-11) in the V1-variable region of the regulatory domain of the PKC molecule. A glutamic acid cluster was located at the carboxyl-terminal side of Ser-11, showing the consensus sequence for phosphorylation by CK-II. The velocity of this phosphorylation was enhanced by the addition of Ca2+, diolein, and phosphatidylserine, which are all required for the activation of PKC. Phosphorylation of casein or synthetic oligopeptides by CK-II was not affected by Ca2+, diolein, or phosphatidylserine. Available evidence suggests that CK-II phosphorylates preferentially the activated form of type II PKC. It remains unknown, however, whether this reaction has a physiological significance.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Tominaga M,Kitagawa Y,Tanaka S,Kishimoto A

doi

10.1093/oxfordjournals.jbchem.a123635

subject

Has Abstract

pub_date

1991-10-01 00:00:00

pages

655-60

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

110

pub_type

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