Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9 |
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Authors: | Elena Tibaldi Heather M Martinez Shunichi Shimasaki Lorenzo A Pinna |
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Institution: | a Department of Biological Chemistry and CNR Neuroscience Institute, University of Padova, Viale G. Colombo, 3, 35131 Padova, Italy b Department of Reproductive Medicine, University of California, San Diego, School of Medicine, La Jolla, CA 92093-0633, USA c Venetian Institute of Molecular Medicine (VIMM), via Orus 2, 35129 Padova, Italy |
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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. |
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Keywords: | Oocyte-secreted factor Phosphorylation Golgi-casein kinase |
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