KOPS - The Institutional Repository of the University of Konstanz

A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6

A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6

Cite This

Files in this item

Checksum: MD5:d7d14886c29ef4b351d581842a1356b1

EBNER, Felix A., Carolin SAILER, Daniela EICHBICHLER, Jasmin JANSEN, Anna SLADEWSKA-MARQUARDT, Florian STENGEL, Martin SCHEFFNER, 2020. A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6. In: Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology. 295(44), pp. 15070-15082. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.ra120.015603

@article{Ebner2020-10-30ubiqu-51165, title={A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6}, year={2020}, doi={10.1074/jbc.ra120.015603}, number={44}, volume={295}, issn={0021-9258}, journal={Journal of Biological Chemistry}, pages={15070--15082}, author={Ebner, Felix A. and Sailer, Carolin and Eichbichler, Daniela and Jansen, Jasmin and Sladewska-Marquardt, Anna and Stengel, Florian and Scheffner, Martin} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/51165"> <dc:creator>Eichbichler, Daniela</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2020-10-02T08:18:18Z</dc:date> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/51165"/> <dc:contributor>Sladewska-Marquardt, Anna</dc:contributor> <dcterms:title>A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6</dcterms:title> <dc:contributor>Jansen, Jasmin</dc:contributor> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/51165/1/Ebner_2-ofhn5oj3ep8j1.pdf"/> <dc:contributor>Ebner, Felix A.</dc:contributor> <dc:language>eng</dc:language> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:contributor>Eichbichler, Daniela</dc:contributor> <dc:contributor>Stengel, Florian</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2020-10-02T08:18:18Z</dcterms:available> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dcterms:issued>2020-10-30</dcterms:issued> <dc:contributor>Scheffner, Martin</dc:contributor> <dcterms:abstract xml:lang="eng">The E6 protein of both mucosal high risk human papillomaviruses (HPVs) such as HPV-16, which have been causally associated with malignant tumors, and low risk HPVs such as HPV-11, which cause the development of benign tumors, interacts with the cellular E3 ubiquitin ligase E6AP. This indicates that both HPV types employ E6AP to organize the cellular proteome to viral needs. However, while several substrate proteins of the high risk E6-E6AP complex are known, e.g. the tumor suppressor p53, potential substrates of the low risk E6-E6AP complex remain largely elusive. Here, we report on an affinity-based enrichment approach that enables the targeted identification of potential substrate proteins of the different E6-E6AP complexes by a combination of E3-selective ubiquitination in whole cell extracts and high-resolution mass spectrometry. The basis for the selectivity of this approach is the use of a ubiquitin variant that is efficiently used by the E6-E6AP complexes for ubiquitination, but not by E6AP alone. By this approach, we identified approximately 190 potential substrate proteins for low risk HPV-11 E6 as well as high risk HPV-16 E6. Moreover, subsequent validation experiments in vitro and within cells with selected substrate proteins demonstrate the potential of our approach. In conclusion, our data represent a reliable repository for potential substrates of the HPV-16 and HPV-11 E6 proteins in complex with E6AP.</dcterms:abstract> <dc:rights>terms-of-use</dc:rights> <dc:creator>Scheffner, Martin</dc:creator> <dc:creator>Jansen, Jasmin</dc:creator> <dc:creator>Sladewska-Marquardt, Anna</dc:creator> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/51165/1/Ebner_2-ofhn5oj3ep8j1.pdf"/> <dc:creator>Stengel, Florian</dc:creator> <dc:creator>Ebner, Felix A.</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:contributor>Sailer, Carolin</dc:contributor> <dc:creator>Sailer, Carolin</dc:creator> </rdf:Description> </rdf:RDF>

Downloads since Oct 2, 2020 (Information about access statistics)

Ebner_2-ofhn5oj3ep8j1.pdf 54

This item appears in the following Collection(s)

Search KOPS


Browse

My Account