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Cyclin-dependent kinase 1–dependent activation of APC/C ubiquitin ligase
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Cyclin-dependent kinase 1–dependent activation of APC/C ubiquitin ligase
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Journal Article
Cyclin-dependent kinase 1–dependent activation of APC/C ubiquitin ligase
2016
Overview
Error-free genome duplication and segregation are ensured through the timely activation of ubiquitylation enzymes. The anaphase-promoting complex or cyclosome (APC/C), a multisubunit E3 ubiquitin ligase, is regulated by phosphorylation. However, the mechanism remains elusive. Using systematic reconstitution and analysis of vertebrate APC/Cs under physiological conditions, we show how cyclin-dependent kinase 1 (CDK1) activates the APC/C through coordinated phosphorylation between Apc3 and Apc1. Phosphorylation of the loop domains by CDK1 in complex with p9/Cks2 (a CDK regulatory subunit) controlled loading of coactivator Cdc20 onto APC/C. A phosphomimetic mutation introduced into Apc1 allowed Cdc20 to increase APC/C activity in interphase. These results define a previously unrecognized subunit-subunit communication over a distance and the functional consequences of CDK phosphorylation. Cdc20 is a potential therapeutic target, and our findings may facilitate the development of specific inhibitors.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Anaphase
/ Animals
/ Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - genetics
/ Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism
/ Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - genetics
/ Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism
/ Enzymes
/ Humans
/ Kinases
/ Mutation
/ Proteins
/ Therapy
/ Xenopus
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