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WEE1B acts as a direct downstream substrate of protein kinase A (PKA) and that Ser (show SIGLEC1 Proteins) 15 of WEE1B is a potential PKA phosphorylation target in the G2/M transition of mouse embryos.
findings demonstrate that exit from metaphase requires not only a proteolytic degradation of cyclin B but also the inhibitory phosphorylation of Cdc2 (show CDK1 Proteins) by Wee1B
Wee1B is a key maturation-promoting-factor inhibitory kinase in mouse oocytes, functions downstream of PKA, and is required for maintaining meiotic arrest.
results suggest pWEE1B is activated after phosphorylation of the Ser77 residue, which is different from phosphorylation site that activates mWEE1B; that pWEE1B is localized in the nucleus; and that the nuclear localization is essential for its function
insufficient amount of Cdc2 and continuous activation of Wee1 B are the cause of meiotic failure of small oocytes in pigs
These results suggest that the inhibitory phosphorylation of CDC2 (show CDK1 Proteins), which is catalyzed by pigWee1B, but not pigMyt1, is involved in the meiotic arrest of porcine oocytes.
Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation.
wee1-like protein kinase 1B
, wee1-like protein kinase 2
, wee1B kinase
, Wee1-like protein kinase 1B
, Wee1-like protein kinase 2
, Wee1B kinase