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Securin
Securin is a protein involved in control of the metaphase-anaphase transition and anaphase onset. Following bi-orientation of chromosome pairs and inactivation of the spindle checkpoint system, the underlying regulatory system, which includes securin, produces an abrupt stimulus that induces highly synchronous chromosome separation in anaphase.
==Securin and Separase==
Securin is initially 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 , inhibiting ubiquitination. When bound to securin, separase is not functional.〔
In addition, both securin and separase are well-conserved proteins (Figure 1).〔 Note that separase cannot function without initially forming the securin-separase complex. This is because securin helps properly fold separase into the functional conformation. However, yeast does not appear to require securin to form functional separase as anaphase occurs in yeast with a securin deletion mutation.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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