What happens if Cdc20 is inhibited?
Anaphase entry requires anaphase-promoting complex/cyclosome (APC/C) activated by co-activator Cdc20, which targets securin and cyclin B for proteasomal degradation via K11-linked polyubiquitination. Securin normally binds and inhibits separase, protease that cleaves cohesin subunit Rad21 holding sister chromatids together. When APC/C-Cdc20 destroys securin, liberated separase removes cohesin, allowing sister chromatids to separate toward opposite poles. If Cdc20 is absent, inhibited by MCC, or chemically blocked, APC/C remains inactive, securin and cyclin B persist, separase stays inhibited,
Ref: Peters, Nature Rev Mol Cell Biol 2006, APC/C and Cdc20; Sivakumar & Gorbsky, Nature Rev Mol Cell Biol 2015, Spindle Checkpoint.