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Golgi apparatus casein kinase phosphorylates bioactive Ser‐6 of bone morphogenetic protein 15 and growth and differentiation factor 9
Author(s) -
Tibaldi Elena,
Arrigoni Giorgio,
Martinez Heather M.,
Inagaki Kenichi,
Shimasaki Shunichi,
Pinna Lorenzo A.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.12.052
Subject(s) - phosphorylation , casein kinase 1 , bone morphogenetic protein 15 , microbiology and biotechnology , casein kinase 2 , growth differentiation factor , golgi apparatus , serine , protein kinase a , bone morphogenetic protein 2 , bone morphogenetic protein , chemistry , biology , biochemistry , kinase , bone morphogenetic protein 7 , cyclin dependent kinase 2 , endoplasmic reticulum , gene , in vitro
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.