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- W2416333604 abstract "Protein ubiquitination involves E1, E2, and E3 trienzyme cascades. E2 and RING E3 enzymes often collaborate to first prime a substrate with a single ubiquitin (UB) and then achieve different forms of polyubiquitination: multiubiquitination of several sites and elongation of linkage-specific UB chains. Here, cryo-EM and biochemistry show that the human E3 anaphase-promoting complex/cyclosome (APC/C) and its two partner E2s, UBE2C (aka UBCH10) and UBE2S, adopt specialized catalytic architectures for these two distinct forms of polyubiquitination. The APC/C RING constrains UBE2C proximal to a substrate and simultaneously binds a substrate-linked UB to drive processive multiubiquitination. Alternatively, during UB chain elongation, the RING does not bind UBE2S but rather lures an evolving substrate-linked UB to UBE2S positioned through a cullin interaction to generate a Lys11-linked chain. Our findings define mechanisms of APC/C regulation, and establish principles by which specialized E3-E2-substrate-UB architectures control different forms of polyubiquitination." @default.
- W2416333604 created "2016-06-24" @default.
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- W2416333604 date "2016-06-01" @default.
- W2416333604 modified "2023-10-17" @default.
- W2416333604 title "Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C" @default.
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- W2416333604 doi "https://doi.org/10.1016/j.cell.2016.05.037" @default.
- W2416333604 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4991212" @default.
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- W2416333604 hasPublicationYear "2016" @default.
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