Recombinant rabbit muscle casein kinase I α is inhibited by heparin and activated by polylysine

Lanmin Zhai, Paul R. Graves, Kenton L. Longenecker, Anna A. DePaoli-Roach, Peter J. Roach

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The casein kinase I (CKI) family consists of widely distributed monomeric Ser/Thr protein kinases that have a preference for acidic substrates. Four mammalian isoforms are known. A full length cDNA encoding the CKIα isoform was cloned from a rabbit skeletal muscle cDNA library and was utilized to construct a bacterial expression vector. Active CKIα was expressed in Escherichia coli as a polypeptide of Mr 36,000. The protein kinase phosphorylated casein, phosvitin and a specific peptide substrate (D4). The enzyme was inhibited by the isoquinolinesulfonamide CKI-7, half-maximally at 70 μM. Heparin inhibited phosphorylation of the D4 peptide or phosvitin by CKIα. Polylysine activated when the D4 peptide was the substrate but had no effect on phosvitin phosphorylation. It is becoming clear that the individual CKI isoforms have different kinetic properties and hence could have quite distinct cellular functions.

Original languageEnglish (US)
Pages (from-to)944-949
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume189
Issue number2
DOIs
StatePublished - Dec 15 1992

Fingerprint

Casein Kinase I
Polylysine
Muscle
Heparin
Phosvitin
Rabbits
Muscles
Peptides
Protein Isoforms
Phosphorylation
Protein Kinases
Substrates
Caseins
Gene Library
Escherichia coli
polylysine-heparin
Skeletal Muscle
Complementary DNA
Kinetics
Enzymes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Recombinant rabbit muscle casein kinase I α is inhibited by heparin and activated by polylysine. / Zhai, Lanmin; Graves, Paul R.; Longenecker, Kenton L.; DePaoli-Roach, Anna A.; Roach, Peter J.

In: Biochemical and Biophysical Research Communications, Vol. 189, No. 2, 15.12.1992, p. 944-949.

Research output: Contribution to journalArticle

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