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000138234 0247_ $$2doi$$a10.1371/journal.pone.0143227
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000138234 037__ $$aDZNE-2020-04556
000138234 041__ $$aEnglish
000138234 082__ $$a610
000138234 1001_ $$0P:(DE-2719)2810402$$aLouis, Marcell$$b0$$eFirst author
000138234 245__ $$aEvolutionary Loss of Activity in De-Ubiquitylating Enzymes of the OTU Family.
000138234 260__ $$aSan Francisco, California, US$$bPLOS$$c2015
000138234 264_1 $$2Crossref$$3online$$bPublic Library of Science (PLoS)$$c2015-11-20
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000138234 520__ $$aUnderstanding function and specificity of de-ubiquitylating enzymes (DUBs) is a major goal of current research, since DUBs are key regulators of ubiquitylation events and have been shown to be mutated in human diseases. Most DUBs are cysteine proteases, relying on a catalytic triad of cysteine, histidine and aspartate to cleave the isopeptide bond between two ubiquitin units in a poly-ubiquitin chain. We have discovered that the two Drosophila melanogaster homologues of human OTUD4, CG3251 and Otu, contain a serine instead of a cysteine in the catalytic OTU (ovarian tumor) domain. DUBs that are serine proteases instead of cysteine- or metallo-proteases have not been described. In line with this, neither CG3251 nor Otu protein were active to cleave ubiquitin chains. Re-introduction of a cysteine in the catalytic center did not render the enzymes active, indicating that further critical features for ubiquitin binding or cleavage have been lost in these proteins. Sequence analysis of OTUD4 homologues from various other species showed that within this OTU subfamily, loss of the catalytic cysteine has occurred frequently in presumably independent events, as well as gene duplications or triplications, suggesting DUB-independent functions of OTUD4 proteins. Using an in vivo RNAi approach, we show that CG3251 might function in the regulation of Inhibitor of Apoptosis (IAP)-antagonist-induced apoptosis, presumably in a DUB-independent manner.
000138234 536__ $$0G:(DE-HGF)POF3-341$$a341 - Molecular Signaling (POF3-341)$$cPOF3-341$$fPOF III$$x0
000138234 542__ $$2Crossref$$i2015-11-20$$uhttp://creativecommons.org/licenses/by/4.0/
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000138234 650_7 $$2NLM Chemicals$$aDrosophila Proteins
000138234 650_7 $$2NLM Chemicals$$aInhibitor of Apoptosis Proteins
000138234 650_7 $$2NLM Chemicals$$aRNA, Small Interfering
000138234 650_7 $$2NLM Chemicals$$aUbiquitin
000138234 650_7 $$2NLM Chemicals$$aotu protein, Drosophila
000138234 650_7 $$0452VLY9402$$2NLM Chemicals$$aSerine
000138234 650_7 $$0EC 3.4.19.12$$2NLM Chemicals$$aOTUD4 protein, human
000138234 650_7 $$0EC 3.4.19.12$$2NLM Chemicals$$aUbiquitin-Specific Proteases
000138234 650_7 $$0K848JZ4886$$2NLM Chemicals$$aCysteine
000138234 650_2 $$2MeSH$$aAmino Acid Sequence
000138234 650_2 $$2MeSH$$aAmino Acid Substitution
000138234 650_2 $$2MeSH$$aAnimals
000138234 650_2 $$2MeSH$$aApoptosis: genetics
000138234 650_2 $$2MeSH$$aBinding Sites
000138234 650_2 $$2MeSH$$aCatalytic Domain
000138234 650_2 $$2MeSH$$aConserved Sequence
000138234 650_2 $$2MeSH$$aCysteine: metabolism
000138234 650_2 $$2MeSH$$aDrosophila Proteins: genetics
000138234 650_2 $$2MeSH$$aDrosophila Proteins: metabolism
000138234 650_2 $$2MeSH$$aDrosophila melanogaster: genetics
000138234 650_2 $$2MeSH$$aDrosophila melanogaster: metabolism
000138234 650_2 $$2MeSH$$aEvolution, Molecular
000138234 650_2 $$2MeSH$$aGene Expression Regulation
000138234 650_2 $$2MeSH$$aHumans
000138234 650_2 $$2MeSH$$aInhibitor of Apoptosis Proteins: antagonists & inhibitors
000138234 650_2 $$2MeSH$$aInhibitor of Apoptosis Proteins: genetics
000138234 650_2 $$2MeSH$$aInhibitor of Apoptosis Proteins: metabolism
000138234 650_2 $$2MeSH$$aMolecular Sequence Data
000138234 650_2 $$2MeSH$$aProtein Binding
000138234 650_2 $$2MeSH$$aRNA, Small Interfering: genetics
000138234 650_2 $$2MeSH$$aRNA, Small Interfering: metabolism
000138234 650_2 $$2MeSH$$aSequence Alignment
000138234 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000138234 650_2 $$2MeSH$$aSerine: metabolism
000138234 650_2 $$2MeSH$$aUbiquitin: genetics
000138234 650_2 $$2MeSH$$aUbiquitin: metabolism
000138234 650_2 $$2MeSH$$aUbiquitin-Specific Proteases: genetics
000138234 650_2 $$2MeSH$$aUbiquitin-Specific Proteases: metabolism
000138234 650_2 $$2MeSH$$aUbiquitination
000138234 7001_ $$0P:(DE-HGF)0$$aHofmann, Kay$$b1
000138234 7001_ $$0P:(DE-2719)2810307$$aBroemer, Meike$$b2$$eLast author
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000138234 8564_ $$uhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0143227
000138234 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4654579
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