Mutual Inhibition of Separase and Cdk1 by Two-Step Complex Formation

Title data

Gorr, Ingo H. ; Boos, Dominik ; Stemmann, Olaf:
Mutual Inhibition of Separase and Cdk1 by Two-Step Complex Formation.
In: Molecular Cell. Vol. 19 (1 July 2005) Issue 1 . - pp. 135-141.
ISSN 1097-4164
DOI: https://doi.org/10.1016/j.molcel.2005.05.022

Official URL:

Abstract in another language

Stable maintenance of genetic information requires chromosome segregation to occur with high accuracy. Anaphase is triggered when ring-shaped cohesin is cleaved by separase, a protease regulated by association with its inhibitor securin. Dispensability of vertebrate securin strongly suggests additional means of separase regulation. Indeed, sister chromatid separation but not securin degradation is inhibited by constitutively active cyclin-dependent kinase 1 (Cdk1) and can be rescued solely by preventing phosphorylation of separase. We demonstrate that Cdk1-dependent phosphorylation of separase is not sufficient for inhibition. In a second step, Cdk1 stably binds phosphorylated separase via its regulatory cyclin B1 subunit. Complex formation results in inhibition of both protease and kinase, and we show that vertebrate separase is a direct inhibitor of Cdk1. This unanticipated function of separase is negatively regulated by securin but independent of separase's proteolytic activity.

Further data

Item Type:	Article in a journal
Refereed:	Yes
Institutions of the University:	Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics > Chair Genetics - Univ.-Prof. Dr. Olaf Stemmann Profile Fields > Advanced Fields > Molecular Biosciences Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics Profile Fields Profile Fields > Advanced Fields Research Institutions Research Institutions > Research Centres
Result of work at the UBT:	No
DDC Subjects:	500 Science > 570 Life sciences, biology
Date Deposited:	27 Mar 2015 07:27
Last Modified:	27 Mar 2015 07:27
URI:	https://eref.uni-bayreuth.de/id/eprint/8554