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ECB-ART-37164
Dev Biol 1999 May 01;2091:200-9. doi: 10.1006/dbio.1999.9248.
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G-protein betagamma subunit-dependent phosphorylation of 62-kDa protein in the early signaling pathway of starfish oocyte maturation induced by 1-methyladenine.

Nakano T , Kontani K , Kurosu H , Katada T , Hoshi M , Chiba K .


Abstract
In starfish oocytes, maturation is induced by a hormone, 1-methyladenine (1-MA), that binds to the receptors exposed to the outer surface of the plasma membrane. The signal of 1-MA stimulates the heterotrimeric G protein, resulting in dissociation of the betagamma subunit of G protein (Gbetagamma) from a pertussis toxin-sensitive Gi-type alpha subunit. To investigate the targets for Gbetagamma, we analyzed 1-MA- or Gbetagamma-dependent phosphorylation using in vivo and in vitro systems. A 62-kDa protein was phosphorylated immediately after 1-MA treatment in intact oocytes. In the cell-free preparations, the 62-kDa protein was also phosphorylated on serine residue(s) immediately after addition of 1-MA or Gbetagamma. The Gbetagamma-dependent phosphorylation of the 62-kDa protein was inhibited by wortmannin or LY294002, which are mechanistically different inhibitors of phosphatidylinositol 3-kinase (PI3K). LY294002 also inhibited Gbetagamma- as well as 1-MA-induced maturation of oocytes. Taken together, these results indicate that the 62-kDa protein functions downstream of Gbetagamma and PI3K in the early signaling pathway of 1-MA-induced starfish oocyte maturation. The phosphorylation of the 62-kDa protein may be required for the activation of maturation-promoting factor.

PubMed ID: 10208753
Article link: Dev Biol


Genes referenced: LOC115919910 LOC586734 LOC588766 pik3ca