Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9

Elena Tibaldi, Giorgio Arrigoni, Heather M. Martinez, Kenichi Inagaki, Shunichi Shimasaki, Lorenzo A. Pinna

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

Bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 (GDF-9) are oocyte-secreted factors that play essential roles in human folliculogenesis and ovulation. Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secretory pathway. Here we show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. rhBMP-15, in particular, is an excellent substrate for G-CK. In each protein a single residue is phosphorylated by G-CK, corresponding to the serine residue at the sixth position of the mature region of both rhBMP-15 and rhGDF-9, whose phosphorylation is required for biological activity.

Original languageEnglish
Pages (from-to)801-805
Number of pages5
JournalFEBS Letters
Volume584
Issue number4
DOIs
Publication statusPublished - Feb 2010
Externally publishedYes

Keywords

  • Golgi-casein kinase
  • Oocyte-secreted factor
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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