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

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.

Pubmed ID: 21186364

Authors

  • Buschhorn BA
  • Petzold G
  • Galova M
  • Dube P
  • Kraft C
  • Herzog F
  • Stark H
  • Peters JM

Journal

Nature structural & molecular biology

Publication Data

January 6, 2011

Associated Grants

  • Agency: Austrian Science Fund FWF, Id: F 3407-B19

Mesh Terms

  • Anaphase-Promoting Complex-Cyclosome
  • Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Apc2 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Apc6 Subunit, Anaphase-Promoting Complex-Cyclosome
  • Cadherins
  • Cdh1 Proteins
  • Cell Cycle Proteins
  • Cytokines
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases
  • Ubiquitination