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dc.contributor.author
Flierman, Dennis
dc.contributor.author
van der Heden van Noort, Gerbrand J.
dc.contributor.author
Ekkebus, Reggy
dc.contributor.author
Geurink, Paul P.
dc.contributor.author
Mevissen, Tycho E.T.
dc.contributor.author
Hospenthal, Manuela
dc.contributor.author
Komander, David
dc.contributor.author
Ovaa, Huib
dc.date.accessioned
2018-11-14T10:05:47Z
dc.date.available
2018-11-08T13:02:16Z
dc.date.available
2018-11-08T17:57:50Z
dc.date.available
2018-11-08T17:59:03Z
dc.date.available
2018-11-08T18:04:29Z
dc.date.available
2018-11-14T10:05:47Z
dc.date.issued
2016-04-26
dc.identifier.issn
2451-9456
dc.identifier.other
10.1016/j.chembiol.2016.03.009
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/301917
dc.identifier.doi
10.3929/ethz-b-000301917
dc.description.abstract
Ubiquitin chains are important post-translational modifications that control a large number of cellular processes. Chains can be formed via different linkages, which determines the type of signal they convey. Deubiquitylating enzymes (DUBs) regulate ubiquitylation status by trimming or removing chains from attached proteins. DUBs can contain several ubiquitin-binding pockets, which confer specificity toward differently linked chains. Most tools for monitoring DUB specificity target binding pockets on opposing sides of the active site; however, some DUBs contain additional pockets. Therefore, reagents targeting additional pockets are essential to fully understand linkage specificity. We report the development of active site-directed probes and fluorogenic substrates, based on non-hydrolyzable diubiquitin, that are equipped with a C-terminal warhead or a fluorogenic activity reporter moiety. We demonstrate that various DUBs in lysates display differential reactivity toward differently linked diubiquitin probes, as exemplified by the proteasome-associated DUB USP14. In addition, OTUD2 and OTUD3 show remarkable linkage-specific reactivity with our diubiquitin-based reagents.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Cell Press
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Non-hydrolyzable Diubiquitin Probes Reveal Linkage-Specific Reactivity of Deubiquitylating Enzymes Mediated by S2 Pockets
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2016-04-07
ethz.journal.title
Cell Chemical Biology
ethz.journal.volume
23
en_US
ethz.journal.issue
4
en_US
ethz.pages.start
472
en_US
ethz.pages.end
482
en_US
ethz.size
12 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.publication.place
Cambridge, MA
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::03412 - Glockshuber, Rudolf / Glockshuber, Rudolf
en_US
ethz.date.deposited
2018-11-08T13:02:18Z
ethz.source
FORM
ethz.eth
no
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2018-11-08T17:57:55Z
ethz.rosetta.lastUpdated
2022-03-28T21:38:48Z
ethz.rosetta.versionExported
true
ethz.COinS
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