Separase

Separin; Esp1; EspL1

Separase is a cysteine protease and endopeptidase belonging to the CD clan protease family. Separase can promote sister chromatid separation by cleaving the Scc1/Rad21 subunit of cohesin. Separase can also cleave Mcd1. Its activity is tightly regulated, and it has complex inhibitory interactions with securin, cyclin B1/CDK1, etc., and is also regulated by PP2A, etc. Separase is closely related to a variety of cancers. In breast cancer, its abnormal expression can predict the prognosis of patients. High mitotic Separase indicates a poor prognosis, while diffuse Separase is associated with a survival advantage. In ovarian cancer, ESPL1 (encoding Separase) is differentially expressed in high-grade serous ovarian cancer, and the expression level is higher than that in normal ovarian tissue. In mouse models, overexpression of Separase can induce aneuploidy and tumorigenesis of mammary epithelial cells. In addition, Separase is also involved in the apoptosis process of yeast cells[1][2][3][4][5][6][7].

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