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

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• 作者：Elena Tibaldi ; Giorgio Arrigoni ; Heather M. Martinez ; Kenichi Inagaki ; Shunichi Shimasaki ; Lorenzo A. Pinna
• 关键词：Oocyte-secreted factor ; Phosphorylation ; Golgi-casein kinase
• 刊名：FEBS Letters
• 出版年：2010
• 出版时间：19 February 2010
• 年：2010
• 卷：584
• 期：4
• 页码：801-805
• 全文大小：466 K

文摘

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.