FAT10, a ubiquitin-independent signal for proteasomal degradation

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HIPP, Mark Steffen, Birte KALVERAM, Shahri RAASI, Marcus GRÖTTRUP, Gunter SCHMIDTKE, 2005. FAT10, a ubiquitin-independent signal for proteasomal degradation. In: Molecular and Cellular Biology. 25(9), pp. 3483-3491. ISSN 0270-7306

@article{Hipp2005-05FAT10-16679, title={FAT10, a ubiquitin-independent signal for proteasomal degradation}, year={2005}, doi={10.1128/MCB.25.9.3483-3491.2005}, number={9}, volume={25}, issn={0270-7306}, journal={Molecular and Cellular Biology}, pages={3483--3491}, author={Hipp, Mark Steffen and Kalveram, Birte and Raasi, Shahri and Gröttrup, Marcus and Schmidtke, Gunter} }

<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/123456789/16679"> <dc:contributor>Schmidtke, Gunter</dc:contributor> <dc:contributor>Raasi, Shahri</dc:contributor> <dcterms:issued>2005-05</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-16T06:49:54Z</dcterms:available> <dc:creator>Schmidtke, Gunter</dc:creator> <dc:contributor>Hipp, Mark Steffen</dc:contributor> <dcterms:abstract xml:lang="eng">FAT10 is a small ubiquitin-like modifier that is encoded in the major histocompatibility complex and is synergistically inducible by tumor necrosis factor alpha and gamma interferon. It is composed of two ubiquitin-like domains and possesses a free C-terminal diglycine motif that is required for the formation of FAT10 conjugates. Here we show that unconjugated FAT10 and a FAT10 conjugate were rapidly degraded by the proteasome at a similar rate. Fusion of FAT10 to the N terminus of very long-lived proteins enhanced their degradation rate as potently as fusion with ubiquitin did. FAT10-green fluorescent protein fusion proteins were not cleaved but entirely degraded, suggesting that FAT10-specific deconjugating enzymes were not present in the analyzed cell lines. Interestingly, the prevention of ubiquitylation of FAT10 by mutation of all lysines or by expression in ubiquitylation-deficient cells did not affect FAT10 degradation. Thus, conjugation with FAT10 is an alternative and ubiquitin-independent targeting mechanism for degradation by the proteasome, which, in contrast to polyubiquitylation, is cytokine inducible and irreversible.</dcterms:abstract> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16679"/> <dc:creator>Hipp, Mark Steffen</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-11-16T06:49:54Z</dc:date> <dc:language>eng</dc:language> <dcterms:bibliographicCitation>Publ. in: Molecular and Cellular Biology ; 25 (2005), 9. - S. 3483-3491</dcterms:bibliographicCitation> <dc:creator>Gröttrup, Marcus</dc:creator> <dc:contributor>Gröttrup, Marcus</dc:contributor> <dc:contributor>Kalveram, Birte</dc:contributor> <dc:creator>Raasi, Shahri</dc:creator> <dc:creator>Kalveram, Birte</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dcterms:title>FAT10, a ubiquitin-independent signal for proteasomal degradation</dcterms:title> </rdf:Description> </rdf:RDF>

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