Show simple item record Tang, W Wu, JQ Chen, C Yang, CS Guo, JY Freel, CD Kornbluth, S
dc.coverage.spatial United States 2011-04-15T16:46:43Z 2010-08-01
dc.identifier E09-08-0708
dc.description.abstract Vertebrate eggs are arrested at Metaphase II by Emi2, the meiotic anaphase-promoting complex/cyclosome (APC/C) inhibitor. Although the importance of Emi2 during oocyte maturation has been widely recognized and its regulation extensively studied, its mechanism of action remained elusive. Many APC/C inhibitors have been reported to act as pseudosubstrates, inhibiting the APC/C by preventing substrate binding. Here we show that a previously identified zinc-binding region is critical for the function of Emi2, whereas the D-box is largely dispensable. We further demonstrate that instead of acting through a "pseudosubstrate" mechanism as previously hypothesized, Emi2 can inhibit Cdc20-dependent activation of the APC/C substoichiometrically, blocking ubiquitin transfer from the ubiquitin-charged E2 to the substrate. These findings provide a novel mechanism of APC/C inhibition wherein the final step of ubiquitin transfer is targeted and raise the interesting possibility that APC/C is inhibited by Emi2 in a catalytic manner.
dc.language eng
dc.language.iso en_US
dc.relation.ispartof Mol Biol Cell
dc.relation.isversionof 10.1091/mbc.E09-08-0708
dc.subject Amino Acid Motifs
dc.subject Anaphase-Promoting Complex-Cyclosome
dc.subject Animals
dc.subject Biocatalysis
dc.subject Enzyme Activation
dc.subject F-Box Proteins
dc.subject Humans
dc.subject Protein Binding
dc.subject Structure-Activity Relationship
dc.subject Substrate Specificity
dc.subject Ubiquitin
dc.subject Ubiquitin-Conjugating Enzymes
dc.subject Ubiquitin-Protein Ligase Complexes
dc.subject Xenopus
dc.subject Xenopus Proteins
dc.title Emi2-mediated inhibition of E2-substrate ubiquitin transfer by the anaphase-promoting complex/cyclosome through a D-box-independent mechanism.
dc.type Journal article
dc.description.version Version of Record 2010-8-1
duke.description.issue 15
duke.description.volume 21
dc.relation.journal Molecular biology of the cell
pubs.begin-page 2589
pubs.end-page 2597
pubs.issue 15
pubs.organisational-group Basic Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Pharmacology & Cancer Biology
pubs.organisational-group School of Medicine
pubs.organisational-group Staff
pubs.publication-status Published
pubs.volume 21
dc.identifier.eissn 1939-4586

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