Show simple item record

dc.contributor.author Tang, W
dc.contributor.author Wu, JQ
dc.contributor.author Chen, C
dc.contributor.author Yang, CS
dc.contributor.author Guo, JY
dc.contributor.author Freel, CD
dc.contributor.author Kornbluth, S
dc.coverage.spatial United States
dc.date.accessioned 2011-04-15T16:46:43Z
dc.date.issued 2010-08-01
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20534816
dc.identifier E09-08-0708
dc.identifier.citation Mol Biol Cell, 2010, 21 (15), pp. 2589 - 2597
dc.identifier.uri http://hdl.handle.net/10161/3328
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.format.extent 2589 - 2597
dc.language eng
dc.language.iso en_US 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 en_US
duke.date.pubdate 2010-8-1 en_US
duke.description.endpage 2597 en_US
duke.description.issue 15 en_US
duke.description.startpage 2589 en_US
duke.description.volume 21 en_US
dc.relation.journal Molecular biology of the cell en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20534816
pubs.issue 15
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Pharmacology & Cancer Biology
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/Staff
pubs.publication-status Published
pubs.volume 21
dc.identifier.eissn 1939-4586

Files in this item

This item appears in the following Collection(s)

Show simple item record