FAT10ylation as a signal for proteasomal degradation


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SCHMIDTKE, Gunter, Annette AICHEM, Marcus GRÖTTRUP, 2014. FAT10ylation as a signal for proteasomal degradation. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843(1), pp. 97-102. ISSN 0167-4889. eISSN 0006-3002

@article{Schmidtke2014-01FAT10-21983, title={FAT10ylation as a signal for proteasomal degradation}, year={2014}, doi={10.1016/j.bbamcr.2013.01.009}, number={1}, volume={1843}, issn={0167-4889}, journal={Biochimica et Biophysica Acta (BBA) - Molecular Cell Research}, pages={97--102}, author={Schmidtke, Gunter and Aichem, Annette and Gröttrup, Marcus} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/21983"> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Aichem, Annette</dc:contributor> <dc:contributor>Gröttrup, Marcus</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-07-23T16:22:57Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-07-23T16:22:57Z</dc:date> <dcterms:issued>2014-01</dcterms:issued> <dc:language>eng</dc:language> <dc:rights>deposit-license</dc:rights> <dc:creator>Schmidtke, Gunter</dc:creator> <dcterms:abstract xml:lang="eng">The Nobel prize has been awarded for the discovery of ubiquitin as a transferable signal for the degradation of proteins by the 26S proteasome. While isopeptide linkage of a protein with a single ubiquitin does not serve as a degradation signal for the proteasome, poly-ubiquitylation via several different lysine residues within ubiquitin leads to efficient proteasomal degradation. Ubiquitin-like modifiers have not been shown to directly mediate proteasomal degradation except for the cytokine inducible modifier HLA-F adjacent transcript 10 (FAT10), which consists of two ubiquitin-like domains. FAT10 ends with a free diglycine motif at its C-terminus which is required for isopeptide linkage to hundreds of different substrates. In contrast to ubiquitin, a single FAT10 suffices to bind to the 26S proteasome and to efficiently mediate proteasomal degradation in a ubiquitin-independent manner. Here we review the data on ubiquitin-independent degradation by FAT10, on how FAT10 is conjugated to its substrates, how FAT10 binds to the 26S proteasome, and how the ubiquitin-like (UBL)-ubiquitin-associated (UBA) protein NUB1L accelerates FAT10 mediated proteolysis. Finally, with a glimpse on recently identified substrates, we will discuss the currently emerging knowledge about the biological functions of FAT10. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System.</dcterms:abstract> <dc:creator>Gröttrup, Marcus</dc:creator> <dc:creator>Aichem, Annette</dc:creator> <dcterms:title>FAT10ylation as a signal for proteasomal degradation</dcterms:title> <dc:contributor>Schmidtke, Gunter</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21983"/> <dcterms:bibliographicCitation>Biochimica et Biophysica Acta (BBA) : Molecular Cell Research ; 1843 (2014), 1. - S. 97-102</dcterms:bibliographicCitation> </rdf:Description> </rdf:RDF>

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