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2021-02-12Zeitschriftenartikel DOI: 10.15252/embj.2020106094
The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63‐branched ubiquitin chains
dc.contributor.authorPluska, Lukas
dc.contributor.authorJarosch, Ernst
dc.contributor.authorZauber, Henrik
dc.contributor.authorKniss, Andreas
dc.contributor.authorWaltho, Anita
dc.contributor.authorBagola, Katrin
dc.contributor.authorvon Delbrück, Maximilian
dc.contributor.authorLöhr, Frank
dc.contributor.authorSchulman, Brenda
dc.contributor.authorSelbach, Matthias
dc.contributor.authorDötsch, Volker
dc.contributor.authorSommer, Thomas
dc.date.accessioned2021-07-22T12:35:10Z
dc.date.available2021-07-22T12:35:10Z
dc.date.issued2021-02-12none
dc.date.updated2021-06-01T13:26:28Z
dc.identifier.issn0261-4189
dc.identifier.urihttp://edoc.hu-berlin.de/18452/23757
dc.description.abstractThe assembly of a specific polymeric ubiquitin chain on a target protein is a key event in the regulation of numerous cellular processes. Yet, the mechanisms that govern the selective synthesis of particular polyubiquitin signals remain enigmatic. The homologous ubiquitin-conjugating (E2) enzymes Ubc1 (budding yeast) and Ube2K (mammals) exclusively generate polyubiquitin linked through lysine 48 (K48). Uniquely among E2 enzymes, Ubc1 and Ube2K harbor a ubiquitin-binding UBA domain with unknown function. We found that this UBA domain preferentially interacts with ubiquitin chains linked through lysine 63 (K63). Based on structural modeling, in vitro ubiquitination experiments, and NMR studies, we propose that the UBA domain aligns Ubc1 with K63-linked polyubiquitin and facilitates the selective assembly of K48/K63-branched ubiquitin conjugates. Genetic and proteomics experiments link the activity of the UBA domain, and hence the formation of this unusual ubiquitin chain topology, to the maintenance of cellular proteostasis.eng
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG) http://dx.doi.org/10.13039/501100001659
dc.description.sponsorshipMax‐Planck‐Gesellschaft (MPG) http://dx.doi.org/10.13039/501100004189
dc.language.isoengnone
dc.publisherHumboldt-Universität zu Berlin
dc.rights(CC BY-NC-ND 4.0) Attribution-NonCommercial-NoDerivatives 4.0 Internationalger
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectcell stresseng
dc.subjectK48‐linkedeng
dc.subjectK63‐linkedeng
dc.subjectpolyubiquitineng
dc.subjectubiquitin‐conjugating enzymeseng
dc.subject.ddc570 Biologienone
dc.titleThe UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63‐branched ubiquitin chainsnone
dc.typearticle
dc.identifier.urnurn:nbn:de:kobv:11-110-18452/23757-6
dc.identifier.doi10.15252/embj.2020106094none
dc.identifier.doihttp://dx.doi.org/10.18452/23113
dc.type.versionpublishedVersionnone
local.edoc.container-titleThe EMBO journalnone
local.edoc.pages19none
local.edoc.type-nameZeitschriftenartikel
local.edoc.institutionLebenswissenschaftliche Fakultätnone
local.edoc.container-publisher-nameWileynone
local.edoc.container-publisher-placeHoboken, NJnone
local.edoc.container-volume40none
local.edoc.container-issue6none
dc.description.versionPeer Reviewednone
local.edoc.container-articlenumbere106094none
dc.identifier.eissn1460-2075

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