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The following table provides information about the project.
UNITED KINGDOM RESEARCH AND INNOVATION
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|Coordinator Country||United Kingdom [UK]|
|Total cost||183˙454 €|
|EC max contribution||183˙454 € (100%)|
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
|Duration (year-month-day)||from 2016-03-01 to 2018-02-28|
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|1||UNITED KINGDOM RESEARCH AND INNOVATION||UK (SWINDON)||coordinator||183˙454.00|
|2||MEDICAL RESEARCH COUNCIL||UK (SWINDON)||coordinator||0.00|
This research proposal describes an ambitious effort to characterize structurally and biochemically ubiquitin chain initiation and elongation by the anaphase-promoting complex or cyclosome (APC/C) in complex with two well-characterized substrates. The APC/C is a multi-subunit cullin-RING E3 ubiquitin ligase that controls progression through the cell cycle by a temporal regulation of its activity and substrate specificity. Regulation and specificity of this E3 ligase is achieved through mutually exclusive binding of two structurally related co-activator subunits termed Cdc20 and Cdh1, as well as through APC/C inhibitors, varying substrate affinities and auto-ubiquitylation of its cognate E2s, namely UbcH10 and Ube2S. In order to understand ubiquitin chain initiation and elongation of the two well-known APC/C substrates cyclin B and securin, I am aiming to use a combined approach of cryo-electron microscopy, X-ray crystallography and a variety of biochemical methods. Within this project I will use cryo-electron microscopy studies to uncover the molecular mechanisms of substrate recognition and ubiquitin chain initiation and elongation by analyzing the APC/CCdh1 co-activator complex bound to its transiently associated E2 enzymes Ube2S or UbcH10 and one of the aforementioned high affinity substrates. Crystallization of selected sub-complexes, namely the catalytic core of the APC/C (composed of Apc2 and Apc11) is intended. If obtained, this high-resolution information will then assist the interpretation of the resulting density maps derived from cryo-electron microscopy.
|year||authors and title||journal||last update|
Andreas Boland, Thomas G Martin, Ziguo Zhang, Jing Yang, Xiao-chen Bai, Leifu Chang, Sjors H W Scheres, David Barford
Cryo-EM structure of a metazoan separaseâ€“securin complex at near-atomic resolution
published pages: 414-418, ISSN: 1545-9993, DOI: 10.1038/nsmb.3386
|Nature Structural & Molecular Biology 24/4||2019-06-13|
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