Structural and functional consequences of NEDD8 phosphorylation

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STUBER, Katrin, Tobias SCHNEIDER, Jill WERNER, Michael KOVERMANN, Andreas MARX, Martin SCHEFFNER, 2021. Structural and functional consequences of NEDD8 phosphorylation. In: Nature Communications. Nature Publishing Group. 12(1), 5939. eISSN 2041-1723. Available under: doi: 10.1038/s41467-021-26189-9

@article{Stuber2021-12Struc-55060, title={Structural and functional consequences of NEDD8 phosphorylation}, year={2021}, doi={10.1038/s41467-021-26189-9}, number={1}, volume={12}, journal={Nature Communications}, author={Stuber, Katrin and Schneider, Tobias and Werner, Jill and Kovermann, Michael and Marx, Andreas and Scheffner, Martin}, note={Article Number: 5939} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Structural and functional consequences of NEDD8 phosphorylation</dcterms:title> <dc:creator>Scheffner, Martin</dc:creator> <dcterms:issued>2021-12</dcterms:issued> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Marx, Andreas</dc:contributor> <dc:creator>Kovermann, Michael</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Scheffner, Martin</dc:contributor> <dspace:isPartOfCollection rdf:resource=""/> <dc:contributor>Stuber, Katrin</dc:contributor> <dspace:hasBitstream rdf:resource=""/> <dc:contributor>Schneider, Tobias</dc:contributor> <dcterms:rights rdf:resource=""/> <dc:contributor>Kovermann, Michael</dc:contributor> <bibo:uri rdf:resource=""/> <dcterms:hasPart rdf:resource=""/> <dc:creator>Stuber, Katrin</dc:creator> <dc:creator>Schneider, Tobias</dc:creator> <dc:rights>terms-of-use</dc:rights> <dcterms:available rdf:datatype="">2021-09-28T11:19:55Z</dcterms:available> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Marx, Andreas</dc:creator> <dc:creator>Werner, Jill</dc:creator> <dc:contributor>Werner, Jill</dc:contributor> <dc:date rdf:datatype="">2021-09-28T11:19:55Z</dc:date> <dcterms:isPartOf rdf:resource=""/> <dcterms:abstract>Ubiquitin (Ub) and Ub-like proteins (Ubls) such as NEDD8 are best known for their function as covalent modifiers of other proteins but they are also themselves subject to post-translational modifications including phosphorylation. While functions of phosphorylated Ub (pUb) have been characterized, the consequences of Ubl phosphorylation remain unclear. Here we report that NEDD8 can be phosphorylated at S65 - the same site as Ub - and that S65 phosphorylation affects the structural dynamics of NEDD8 and Ub in a similar manner. While both pUb and phosphorylated NEDD8 (pNEDD8) can allosterically activate the Ub ligase Parkin, they have different protein interactomes that in turn are distinct from those of unmodified Ub and NEDD8. Among the preferential pNEDD8 interactors are HSP70 family members and we show that pNEDD8 stimulates HSP70 ATPase activity more pronouncedly than unmodified NEDD8. Our findings highlight the general importance of Ub/NEDD8 phosphorylation and support the notion that the function of pUb/pNEDD8 does not require their covalent attachment to other proteins.</dcterms:abstract> </rdf:Description> </rdf:RDF>

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