Answer
This decrease in M-cyclin concentration causes M-Cdk to become inactive, which causes a large number of substrates that had previously been phosphorylated by the active M-Cdk to become dephosphorylated.
Work Step by Step
M-Cdk activity activates the APC/C, which in turn mediates the proteolysis of cyclin B. A rapid drop in the quantity of M-cyclin is caused by the APC/targeting C's of cyclin B for ubiquitination and subsequent proteasome destruction.
PP1 and PP2A are two examples of protein phosphatases that can facilitate the dephosphorylation of M-cyclin. The binding of regulatory subunits and modifications in subcellular localization are two of the many ways that can activate these phosphatases. M-cyclin is inactivated and subsequently degraded as a result of dephosphorylation.
