Cybip, a starfish cyclin B-binding protein, is involved in meiotic M-phase exit

Biochem Biophys Res Commun. 2003 Jan 3;300(1):121-7. doi: 10.1016/s0006-291x(02)02797-3.

Abstract

We designed a screen to identify starfish oocyte proteins able to bind monomeric cyclin B by affinity chromatography on a cyclin B splice variant displaying low affinity for cdc2. We identified a 15kDa protein previously described as a cdk-binding protein [Biochim. Biophys. Acta Mol. Cell Res. 1589 (2002) 219-231]. Cybip is encoded by a single polymorphic gene and the native protein is matured by cleaving a signal peptide. We firmly establish the fact that it is a true cyclin B-binding protein, since the recombinant protein binds recombinant cyclin B in absence of any cdk. Finally, we show that the microinjection of GST-cybip, and of anti-cybip antibody, in maturing starfish oocytes, inhibits H1 kinase and MPF inactivation, and first polar body emission.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Chromatography, Affinity
  • Cyclin B / metabolism*
  • Female
  • Maturation-Promoting Factor / metabolism
  • Meiosis / genetics
  • Meiosis / physiology*
  • Molecular Sequence Data
  • Molecular Weight
  • Oocytes / cytology
  • Oocytes / metabolism
  • Polymorphism, Genetic
  • Protein Isoforms / genetics
  • Protein Isoforms / isolation & purification
  • Protein Isoforms / metabolism
  • Sequence Homology, Amino Acid
  • Starfish / cytology
  • Starfish / genetics
  • Starfish / metabolism*

Substances

  • Carrier Proteins
  • Cyclin B
  • Protein Isoforms
  • Maturation-Promoting Factor