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UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex.

http://www.ncbi.nlm.nih.gov/pubmed/20080579

The Anaphase-Promoting Complex (APC) is an E3 ubiquitin ligase that regulates mitosis and G1 by sequentially targeting cell-cycle regulators for ubiquitination and proteasomal degradation. The mechanism of ubiquitin chain formation by APC and the resultant chain topology remains controversial. By using a single-lysine APC substrate to dissect the topology of ubiquitinated substrates, we find that APC-catalyzed ubiquitination has an intrinsic preference for the K11 linkage of ubiquitin that is essential for substrate degradation. K11 specificity is determined by an E2 enzyme, UBE2S/E2-EPF, that elongates ubiquitin chains after the substrates are pre-ubiquitinated by UbcH10 or UbcH5. UBE2S copurifies with APC; dominant-negative Ube2S slows down APC substrate degradation in functional cell-cycle extracts. We propose that Ube2S is a critical, unique component of the APC ubiquitination pathway.

Pubmed ID: 20080579 RIS Download

Mesh terms: Anaphase-Promoting Complex-Cyclosome | Biocatalysis | Cell Cycle | HeLa Cells | Humans | Lysine | Mutation | Neoplasm Proteins | Protein Binding | Securin | Substrate Specificity | Ubiquitin | Ubiquitin-Conjugating Enzymes | Ubiquitin-Protein Ligase Complexes

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Associated grants

  • Agency: NIGMS NIH HHS, Id: 5R01GM39023-21

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