Anaphase specific auto‐cleavage of separase

FEBS Letters

Mann, Matthias²  Anderson, Jens S²  Zou, Hui³  Stemman, Olaf¹  Kirschner, Marc W⁴ 

[1] Max-Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18a, 82152 Martinsried, Germany;Protein Interaction Laboratory, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark;Department of Molecular Biology, UT Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd., Dallas, TX 75390, USA;Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA

关键词: Separase;    Securin;    Chromatid separation;    Anaphase;    Cysteine protease;   

DOI  :  10.1016/S0014-5793(02)03238-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sister-chromatid separation is triggered by a specific proteolytic cleavage of chromosomal cohesins catalyzed by the endopeptidase separase. Prior to anaphase, separase is inhibited independently by affinity binding to securin and by specific inhibitory phosphorylation. Here we show that separase itself is also subjected to proteolytic cleavages at three adjacent sites. The cleavages are auto-catalyzed and occur specifically at anaphase coincident with separase activation. The cleaved fragments remain associated with each other and are catalytically active. Mapping of the cleavage sites reveals that all three sites are conserved in vertebrates underlining a significant function for this regulation.

【 授权许可】

Unknown