Separase

Separase also known as separin is a cysteine protease responsible for triggering anaphase by hydrolysing cohesin which is the protein responsible for binding sister chromatids during metaphase. In humans, separin is encoded by the ESPL1 gene.

Read more about Separase:  Discovery, Function, Regulation

Other articles related to "separase":

MAD2 - Metaphase-to-anaphase Transition
... and activates its bound protease partner, separase ... Separase bound to securin remains inhibited however, when inhibition is relieved, activated separase cleaves the cohesin complex which links the sister chromatids together ...
Role of Securin in The Onset of Anaphase - Network Characteristics
... integrates multiple regulatory inputs to make separase activation switch-like, resulting in sudden, coordinated anaphase ... behavior contains a positive feedback loop for activation of Cdc14 by separase, leading to dephosphorylation and degradation of securin (Figure 3) ... This means that strong inactivation of separase by securin followed by sudden, rapid destruction of securin and activation of separase is vital for proper ...
Separase - Regulation
... When the cell is not dividing, separase is prevented from cleaving cohesin through its association with another protein, securin, as well as phosphorylation by the cyclin-CDK complex ... Interestingly, separase cannot function without initially forming the securin-separase complex in most organisms ... This is because securin helps properly fold separase into the functional conformation ...
Securin and Separase
... present in the cytoplasm and binds to separase, a protease that degrades the cohesin rings that link the two sister chromatids ... Separase is vital for onset of anaphase ... This securin-separase complex is maintained when securin is phosphorylated by Cdk1, inhibiting ubiquitination ...