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- Title
Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1.
- Authors
Buschhorn, Bettina A; Petzold, Georg; Galova, Marta; Dube, Prakash; Kraft, Claudine; Herzog, Franz; Stark, Holger; Peters, Jan-Michael
- Abstract
The anaphase-promoting complex/cyclosome (APC/C) is a 22S ubiquitin ligase complex that initiates chromosome segregation and mitotic exit. We have used biochemical and electron microscopic analyses of Saccharomyces cerevisiae and human APC/C to address how the APC/C subunit Doc1 contributes to recruitment and processive ubiquitylation of APC/C substrates, and to understand how APC/C monomers interact to form a 36S dimeric form. We show that Doc1 interacts with Cdc27, Cdc16 and Apc1 and is located in the vicinity of the cullin-RING module Apc2-Apc11 in the inner cavity of the APC/C. Substrate proteins also bind in the inner cavity, in close proximity to Doc1 and the coactivator Cdh1, and induce conformational changes in Apc2-Apc11. Our results suggest that substrates are recruited to the APC/C by binding to a bipartite substrate receptor composed of a coactivator protein and Doc1.
- Publication
Nature structural & molecular biology, 2011, Vol 18, Issue 1, p6
- ISSN
1545-9985
- Publication type
Journal Article
- DOI
10.1038/nsmb.1979