Literature DB >> 6576911

Autophosphorylation of type 2 casein kinase TS at both its alpha- and beta-subunits. Influence of different effectors.

F Meggio, A M Brunati, L A Pinna.   

Abstract

Rat liver casein kinase TS (Ck-TS) having quaternary structure alpha 2 beta 2, autophosphorylates at its 25 kDa, beta-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 beta-subunit; (ii) stimulators possessing several amino groups (like spermine) which increase the autophosphorylation at the beta-subunit; (iii) stimulators possessing several guanido groups, like protamines and related peptides, which prevent the phosphorylation of the beta-subunit, while promoting the autophosphorylation of the 38 kDa alpha-subunit. In the presence of such polyarginyl effectors the 130 kDa Ck-TS is converted into forms with higher sedimentation coefficient.

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Year:  1983        PMID: 6576911     DOI: 10.1016/0014-5793(83)80967-3

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  15 in total

1.  Functional analysis of CK2beta-derived synthetic fragments.

Authors:  F Meggio; O Marin; S Sarno; L A Pinna
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

2.  Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance.

Authors:  M J Benitez; G Mier; F Brione; F J Moreno; J S Jiménez
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

3.  Autocatalytic tyrosine-phosphorylation of protein kinase CK2 alpha and alpha' subunits: implication of Tyr182.

Authors:  A Donella-Deana; L Cesaro; S Sarno; A M Brunati; M Ruzzene; L A Pinna
Journal:  Biochem J       Date:  2001-07-15       Impact factor: 3.857

4.  Evidence that insulin activates casein kinase 2 in rat epididymal fat-cells and that this may result in the increased phosphorylation of an acid-soluble 22 kDa protein.

Authors:  T A Diggle; C Schmitz-Peiffer; A C Borthwick; G I Welsh; R M Denton
Journal:  Biochem J       Date:  1991-10-15       Impact factor: 3.857

5.  Phosphorylation of cytosolic proteins by casein kinases in human erythrocytes. Response to ionic strength and to 2,3-bisphosphoglycerate.

Authors:  G Clari; V Moret
Journal:  Mol Cell Biochem       Date:  1987-04       Impact factor: 3.396

Review 6.  Protein kinases phosphorylating acidic ribosomal proteins from yeast cells.

Authors:  R Szyszka
Journal:  Folia Microbiol (Praha)       Date:  1999       Impact factor: 2.099

7.  A surface-plasmon-resonance analysis of polylysine interactions with a peptide substrate of protein kinase CK2 and with the enzyme.

Authors:  M J Benítez; G Mier; F Briones; F J Moreno; J S Jiménez
Journal:  Biochem J       Date:  1997-06-15       Impact factor: 3.857

8.  Inhibition of rat heart ornithine decarboxylase by basic polypeptides.

Authors:  F Flamigni; C Guarnieri; S Marmiroli; C M Caldarera
Journal:  Biochem J       Date:  1985-08-01       Impact factor: 3.857

9.  The effect of amino acids, monoamines and polyamines on pyruvate dehydrogenase activity in mitochondria from rat adipocytes.

Authors:  F L Kiechle; H Malinski; D M Dandurand; J B McGill
Journal:  Mol Cell Biochem       Date:  1990-03-27       Impact factor: 3.396

10.  A polylysine-induced aggregation of substrate accompanies the stimulation of casein kinase II by polylysine.

Authors:  F J Moreno; C G Lechuga; M Collado; M J Benítez; J S Jiménez
Journal:  Biochem J       Date:  1993-02-01       Impact factor: 3.857

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