Substrate binding on the APC/C occurs between the coactivator Cdh1 and the processivity factor Doc1

Bettina A. Buschhorn, Georg Petzold, Marta Galova, Prakash Dube, Claudine Kraft, Franz Herzog, Holger Stark, Jan Michael Peters

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

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.

OriginalspracheEnglisch
Seiten (von - bis)6-13
Seitenumfang8
FachzeitschriftNature Structural and Molecular Biology
Jahrgang18
Ausgabenummer1
DOIs
PublikationsstatusVeröffentlicht - Jän. 2011
Extern publiziertJa

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