In "S. cerevisiae", Pds1p (also known as securin) regulates sister chromatids cohesion, because it binds and inhibits the protease Esp1p (separin or separase). When anaphase onset is triggered, the anaphase-promoting complex (APC/C or Cyclosome) degrades securin. APC/C is a ring E3 ubiquitin ligase that recruits an E2 ubiquitin-conjugating enzyme loaded with ubiquitin. Securin is recognized only if Cdc20, the activator subunit, is bound to the APC/C core. When securin, Cdc20, and E2 are all bound to APC/C E2 ubiquitinates securin and selectively degrades it. Securin degradation releases the protease Esp1p/separase, which degrades the cohesin rings that link the two sister chromatids, therefore promoting sister chromatids separation. It has been also shown that Polo/Cdc5 kinase phosphorylates serine residues next to the cutting site for Scc1, and this phosphorylation would facilitate the cutting activity.