Specific kinase proteins responsible for activation or degradation of CTNNB1, glycogen synthase kinase-3β (GSK3β) phosphorylate Ser33, Ser37 and Thr41 residues in order degrade CTNNB1. Similarly, casein kinase-1 (CK1) at Ser45 residue (Fang et al., 2007). Activation CTNNB1 happen …show more content…
CTNNB1 deficiency results in infertile female mice, even though mice show normal ovarian function. Results indicate that FSH mediated steroidogenesis regulation requires CTNNB1. Beta-catenin deactivation under the effect of LH has been improved (Roy et al., 2009) at the bovine luteal cells as a model of study. Beta-catenin as an essential transcriptional regulator of CYP19A1, CTNNB1alteration level is sensitive for regulation of FSH and cAMP-dependent promoters, CTNNB1 has a stimulatory effect that mediated within functional interactions with Steroidogenic factor-1 (Parakh et al., …show more content…
Furthermore, Roy et al, (2009). Indicated that luteinizing Hormone (LH) on luteal cells can directly phosphorylate GSK3β through PKA-dependent phosphorelation, and that 's reflected in the accumulation of CTNNB1 and the StAR enzyme synthesis. Although, treatment with FSH increase AKT abundance which increase E2 synthesis, the activation of this pathway induces the phosphorelation of GSK3β that consider one part of the CTNNB1 destruction complex (Law et al., 2013), related of what Gomez et al., (2015) recently found that AKT is required in CTNNB1 regulation and ovarian estrogen synthesis in bovine granulosa cells. But further researches still required to evaluate the role of AKT in human ovarian granulosa cells and wither GSK3β directly phosphorelate by