BIOL 201 Lecture Notes - Lecture 29: Microtubule, Cdc20, Separase
Document Summary
Degrading cyclins to reset the timer for the next mitosis. Proteins are degraded by a complex known as the proteasome after they have been tagged by poly-ubiquitination. This tagging allows the proteins to be recognized by the proteasome for degradation. It targets a bunch of proteins exiting mitosis. Apc gets its specificity and activation from binding partners. These activators in the cytoplasm bind to the apc and then the apc goes to get ubiquitinated. Cells hold back the metaphase-anaphase transition by inhibiting apc partners. Cdc20 binds to the apc and targets/activates it for ubiquitination. This ubiquitination event is what brings the chromosomes apart. After anaphase, cdh1 binds to the apc and. Cdc20 needs to be controlled since anaphase has to wait for the chromosomes to be bi- oriented on the spindle. Ring of cohesive molecule hold together the sister chromatids. Scc1 gets cleaved by separase, so you would have to prevent separase from cleaving while waiting.