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XB-ART-34933
EMBO J. December 13, 2006; 25 (24): 5716-25.

Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation.

Han SJ , Vaccari S , Nedachi T , Andersen CB , Kovacina KS , Roth RA , Conti M .


Abstract
cGMP-inhibited cAMP phosphodiesterase 3A (PDE3A) is expressed in mouse oocytes, and its function is indispensable for meiotic maturation as demonstrated by genetic ablation. Moreover, PDE3 activity is required for insulin/insulin-like growth factor-1 stimulation of Xenopus oocyte meiotic resumption. Here, we investigated the cAMP-dependent protein kinase B (PKB)/Akt regulation of PDE3A and its impact on oocyte maturation. Cell-free incubation of recombinant mouse PDE3A with PKB/Akt or cAMP-dependent protein kinase A catalytic subunits leads to phosphorylation of the PDE3A protein. Coexpression of PDE3A with constitutively activated PKB/Akt (Myr-Akt) increases PDE activity as well as its phosphorylation state. Injection of pde3a mRNA potentiates insulin-dependent maturation of Xenopus oocytes and rescues the phenotype of pde3(-/-) mouse oocytes. This effect is greatly decreased by mutation of any of the PDE3A serines 290-292 to alanine in both Xenopus and mouse. Microinjection of myr-Akt in mouse oocytes causes in vitro meiotic maturation and this effect requires PDE3A. Collectively, these data indicate that activation of PDE3A by PKB/Akt-mediated phosphorylation plays a role in the control of PDE3A activity in mammalian oocytes.

PubMed ID: 17124499
PMC ID: PMC1698880
Article link: EMBO J.
Grant support: U54 HD 31398 NICHD NIH HHS

Genes referenced: akt1 ins pde3a ptk2b
Antibodies referenced:

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