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

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.

Pubmed ID: 11562349

Authors

  • Pfleger CM
  • Lee E
  • Kirschner MW

Journal

Genes & development

Publication Data

September 15, 2001

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM26875
  • Agency: NIGMS NIH HHS, Id: GM39023

Mesh Terms

  • 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