Stereospecific phosphorylation by the central mitotic kinase Cdk1-cyclin B

ACS Chem Biol. 2015 Apr 17;10(4):952-6. doi: 10.1021/cb500815b. Epub 2015 Jan 26.

Abstract

The cis vs trans conformation, or shape, of phosphoserine-proline (pSer-Pro), a prevalent motif in cell cycle proteins, may play a significant role in regulating mitosis. We demonstrate that Cdk1-cyclin B, the central mitotic kinase, is specific for the trans conformation, not cis, of synthetic, locked Ser-Pro 11-residue peptide substrates, using LC-MSMS detection and sequencing of phosphorylated products. This substrate stereospecificity may contribute an additional level of mitotic regulation.

Publication types

  • Letter
  • Research Support, N.I.H., Extramural

MeSH terms

  • CDC2 Protein Kinase
  • Cyclin B1 / chemistry*
  • Cyclin B1 / metabolism*
  • Cyclin-Dependent Kinases / chemistry*
  • Cyclin-Dependent Kinases / metabolism*
  • Mitosis
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptides / chemistry
  • Peptides / metabolism
  • Peptidylprolyl Isomerase / metabolism
  • Phosphorylation
  • Protein Conformation
  • Solid-Phase Synthesis Techniques
  • Stereoisomerism
  • Tandem Mass Spectrometry

Substances

  • CCNB1 protein, human
  • Cyclin B1
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptides
  • CDC2 Protein Kinase
  • CDK1 protein, human
  • Cyclin-Dependent Kinases
  • PIN1 protein, human
  • Peptidylprolyl Isomerase