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Background
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ESPL1 is a caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms. ESPL1 is regulated by at least two independent mechanisms. First, it is inactivated via its interaction with securin/PTTG1, which probably covers its active site. The association with PTTG1 is not only inhibitory, since PTTG1 is also required for activating it, the enzyme being inactive in cells in which PTTG1 is absent. PTTG1 degradation at anaphase, liberates it and triggers RAD21 cleavage. Second, phosphorylation at Ser-1126 inactivates it. The complete phosphorylation during mitosis, is removed when cells undergo anaphase. Activation of the enzyme at the metaphase-anaphase transition probably requires the removal of both securin and inhibitory phosphate.
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Background
References
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- Beausoleil, S.A., et al., Proc. Natl. Acad. Sci. U.S.A. 101(33):12130-12135 (2004).
- Chestukhin, A., et al., Proc. Natl. Acad. Sci. U.S.A. 100(8):4574-4579 (2003).
- Chen, F., et al., J. Biol. Chem. 277(19):16775-16781 (2002).
- Waizenegger, I., et al., Curr. Biol. 12(16):1368-1378 (2002).
- Hauf, S., et al., Science 293(5533):1320-1323 (2001).
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