Phosphoserine in peptide substrates can specify casein kinase II action

T. W. Hrubey, P. J. Roach

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

Casein kinase II is a ubiquitous serine/threonine protein kinase which utilizes acidic amino acid residues as recognition determinants in its substrates, the motif -S/T-X-X-D/E- being particularly important. To test whether a phosphoserine residue can act as a substrate determinant, a peptide was synthesized, containing the sequence -S-X-X-S, which was not phosphorylated by casein kinase II. However, upon phosphorylation at the +3 position, the peptide became a substrate for casein kinase II. With another peptide, a positive influence of more distal phosphorylations was found. The results indicate the potential for casein kinase II to participate in hierarchal phosphorylation schemes.

Original languageEnglish (US)
Pages (from-to)190-196
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume172
Issue number1
DOIs
StatePublished - Oct 15 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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