Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex.

Pfleger CM, Lee E, Kirschner MW
Genes Dev. 2001 15 (18): 2396-407

PMID: 11562349 · PMCID: PMC312782 · DOI:10.1101/gad.918201

The specificity of ubiquitin-mediated protein degradation with regards to the selection of substrates to be polyubiquitinated has only been determined rather recently. Substrate targeting by the N-end rule and HECT (homology to E6AP carboxyl terminus) domain ubiquitin ligases occurs through substrate-specific binding domains. In contrast, the SCF complex recruits substrates through a substrate adaptor protein, the F-box subunit. Despite evidence showing that Cdc20 and Cdh1 bind and activate the anaphase-promoting complex (APC) in a substrate-specific manner, there is no evidence that the activating protein and substrate interact directly; hence, no clear model exists for the mechanism of APC activation or recruitment of substrates. We show here that the activators Cdc20 and Cdh1 can associate with substrates via their N termini. In the absence of APC, Cdc20 and Cdh1 bind substrates reflecting Cdc20-APC and Cdh1-APC specificity. The N termini of Cdc20 and Cdh1 provide specificity functionally, as demonstrated by the generation of active chimeras that display the specificity corresponding to their N termini. Thus, Cdc20 and Cdh1 act as both substrate recognition and activating modules for APC.

MeSH Terms (13)

Amino Acid Sequence Anaphase-Promoting Complex-Cyclosome Cdc20 Proteins Cdh1 Proteins Cell Cycle Proteins Fungal Proteins Ligases Molecular Sequence Data Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Substrate Specificity Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases

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