Phosphorylation of K-casein by glycogen synthase kinase-3 from rabbit skeletal muscle

Arianna Donella-Deana; Lorenza A. Pinna; Brian Hemmings; Philip Cohen

doi:10.1016/0167-4838(83)90043-2

Phosphorylation of K-casein by glycogen synthase kinase-3 from rabbit skeletal muscle

Arianna Donella-Deana, Lorenza A. Pinna, Brian Hemmings, Philip Cohen

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

2 Citations (Scopus)

Abstract

Glycogen synthase kinase-3 (ATP: protein phosphotransferase, EC 2.7.1.37) phosphorylated K-casein 20-fold more rapidly than β-casein, while α_S1-casein was not a substrate. This distinguished it from casein kinase-I and casein kinase-II, which phosphorylate the β-casein variant preferentially. Glycogen synthase kinase-3 phosphorylated a serine residue(s) in the C-terminal cyanogen bromide fragment on K-casein. In contrast, cyclic AMP-dependent protein kinase phosporylated the N-terminal fragment, and phosphorylase kinase the N-terminal and intermediate cyanogen bromide fragments. The results emphasize the potential value of casein phosphorylation as a means of classifying protein kinases.

Original language	English
Pages (from-to)	149-153
Number of pages	5
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	745
Issue number	2
DOIs	https://doi.org/10.1016/0167-4838(83)90043-2
Publication status	Published - 15 Jun 1983

Keywords

(Rabbit skeletal muscle)
Casein kinase
Glycogen synthase kinase
Protein kinase

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology

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title = "Phosphorylation of K-casein by glycogen synthase kinase-3 from rabbit skeletal muscle",

abstract = "Glycogen synthase kinase-3 (ATP: protein phosphotransferase, EC 2.7.1.37) phosphorylated K-casein 20-fold more rapidly than β-casein, while αS1-casein was not a substrate. This distinguished it from casein kinase-I and casein kinase-II, which phosphorylate the β-casein variant preferentially. Glycogen synthase kinase-3 phosphorylated a serine residue(s) in the C-terminal cyanogen bromide fragment on K-casein. In contrast, cyclic AMP-dependent protein kinase phosporylated the N-terminal fragment, and phosphorylase kinase the N-terminal and intermediate cyanogen bromide fragments. The results emphasize the potential value of casein phosphorylation as a means of classifying protein kinases.",

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AU - Donella-Deana, Arianna

AU - Pinna, Lorenza A.

AU - Hemmings, Brian

AU - Cohen, Philip

PY - 1983/6/15

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N2 - Glycogen synthase kinase-3 (ATP: protein phosphotransferase, EC 2.7.1.37) phosphorylated K-casein 20-fold more rapidly than β-casein, while αS1-casein was not a substrate. This distinguished it from casein kinase-I and casein kinase-II, which phosphorylate the β-casein variant preferentially. Glycogen synthase kinase-3 phosphorylated a serine residue(s) in the C-terminal cyanogen bromide fragment on K-casein. In contrast, cyclic AMP-dependent protein kinase phosporylated the N-terminal fragment, and phosphorylase kinase the N-terminal and intermediate cyanogen bromide fragments. The results emphasize the potential value of casein phosphorylation as a means of classifying protein kinases.

AB - Glycogen synthase kinase-3 (ATP: protein phosphotransferase, EC 2.7.1.37) phosphorylated K-casein 20-fold more rapidly than β-casein, while αS1-casein was not a substrate. This distinguished it from casein kinase-I and casein kinase-II, which phosphorylate the β-casein variant preferentially. Glycogen synthase kinase-3 phosphorylated a serine residue(s) in the C-terminal cyanogen bromide fragment on K-casein. In contrast, cyclic AMP-dependent protein kinase phosporylated the N-terminal fragment, and phosphorylase kinase the N-terminal and intermediate cyanogen bromide fragments. The results emphasize the potential value of casein phosphorylation as a means of classifying protein kinases.

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KW - Glycogen synthase kinase

KW - Protein kinase

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Phosphorylation of K-casein by glycogen synthase kinase-3 from rabbit skeletal muscle

Abstract

Keywords

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