Autophosphorylation of type 2 casein kinase TS at both its α‐ and β‐subunits
- 22 August 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 160 (1-2), 203-208
- https://doi.org/10.1016/0014-5793(83)80967-3
Abstract
Rat liver casein kinase TS (Ck‐TS) having quarternary structure α2β2, autophosphorylates at its 25 kDa, β‐subunits, incorporating up to 1.2 mol P/mol enzyme. According to their effects on the autophosphorylation pattern the effectors of Ck‐TS activity can be grouped into 3 classes: (i) inhibitors, like heparin, which also prevent the autophosphorylation of the β‐subunit; (ii) stimulators possessing several amino groups (like spermine) which increase the autophosphorylation at the β‐subunit; (iii) stimulators possessing several guanido groups, like protamines and related peptides, which prevent the phosphorylation of the β‐subunit, while promoting the autophosphorylation of the 38 kDa α‐subunit. In the presence of such polyarginyl effectors the 130 kDa Ck‐TS is converted into forms with higher sedimentation coefficient.Keywords
This publication has 21 references indexed in Scilit:
- Catalytic and molecular properties of a highly purified G type casein kinase from bovine lung tissueBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Phosphorylation of the Type‐II Regulatory Subunit of Cyclic‐AMP‐Dependent Protein Kinase by Glycogen Synthase Kinase 3 and Glycogen Synthase Kinase 5European Journal of Biochemistry, 1982
- Isolation and characterization of a Type II casein kinase (‘casein kinase‐TS’) from Saccharomyces cerevisiaeFEBS Letters, 1982
- Inhibition of rat liver cytosol casein kinases by heparinFEBS Letters, 1982
- Polyamines alter the substrate preference of nuclear protein kinase NIIBiochemistry, 1982
- Phosphorylation of troponin T by casein kinase TSBiochemical and Biophysical Research Communications, 1981
- Cyclic nucleotide independent casein kinase (G type) in bovine adrenal cortex Purification and properties of two molecular formsBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Selective inhibition of a cyclic nucleotide‐independent protein kinase (G‐type casein kinase) by naturally occurring glycosaminoglycansFEBS Letters, 1980
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970