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TitleMechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly.
Journal, issue, pagesMol Cell, Vol. 56, Issue 2, Page 246-260, Year 2014
Publish dateOct 23, 2014
AuthorsNicholas G Brown / Edmond R Watson / Florian Weissmann / Marc A Jarvis / Ryan VanderLinden / Christy R R Grace / Jeremiah J Frye / Renping Qiao / Prakash Dube / Georg Petzold / Shein Ei Cho / Omar Alsharif / Ju Bao / Iain F Davidson / Jie J Zheng / Amanda Nourse / Igor Kurinov / Jan-Michael Peters / Holger Stark / Brenda A Schulman /
PubMed AbstractPolyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein function. Some RING E3s, including anaphase-promoting complex/cyclosome (APC), catalyze polyubiquitination by ...Polyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein function. Some RING E3s, including anaphase-promoting complex/cyclosome (APC), catalyze polyubiquitination by sequential reactions with two different E2s. An initiating E2 ligates ubiquitin to an E3-bound substrate. Another E2 grows a polyubiquitin chain on the ubiquitin-primed substrate through poorly defined mechanisms. Here we show that human APC's RING domain is repurposed for dual functions in polyubiquitination. The canonical RING surface activates an initiating E2-ubiquitin intermediate for substrate modification. However, APC engages and activates its specialized ubiquitin chain-elongating E2 UBE2S in ways that differ from current paradigms. During chain assembly, a distinct APC11 RING surface helps deliver a substrate-linked ubiquitin to accept another ubiquitin from UBE2S. Our data define mechanisms of APC/UBE2S-mediated polyubiquitination, reveal diverse functions of RING E3s and E2s, and provide a framework for understanding distinctive RING E3 features specifying ubiquitin chain elongation.
External linksMol Cell / PubMed:25306923 / PubMed Central
MethodsEM (single particle) / NMR (solution) / X-ray diffraction
Resolution1.755 - 23.0 Å
Structure data

EMDB-2775:
Mechanism of polyubiquitination by human Anaphase Promoting Complex: RING repurposing for ubiquitin chain assembly
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-6084:
Anaphase Promoting Complex with bound Ube2S
Method: EM (single particle) / Resolution: 23.0 Å

PDB-2mt5:
Isolated Ring domain
Method: SOLUTION NMR

PDB-4r2y:
Crystal structure of APC11 RING domain
Method: X-RAY DIFFRACTION / Resolution: 1.755 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • unidentified (others)
KeywordsMETAL BINDING PROTEIN / Ring domain / zinc binding domain / LIGASE / E3 Ubiquitin Ligase

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