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Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase

Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase

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RUBENSTEIN, Eric M., Stefan G. KREFT, Wesley GREENBLATT, Robert SWANSON, Mark HOCHSTRASSER, 2012. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. In: The Journal of Cell Biology. 197(6), pp. 761-773. ISSN 0021-9525. eISSN 1540-8140

@article{Rubenstein2012-06-11Aberr-21018, title={Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase}, year={2012}, doi={10.1083/jcb.201203061}, number={6}, volume={197}, issn={0021-9525}, journal={The Journal of Cell Biology}, pages={761--773}, author={Rubenstein, Eric M. and Kreft, Stefan G. and Greenblatt, Wesley and Swanson, Robert and Hochstrasser, Mark} }

<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/123456789/21018"> <dcterms:issued>2012-06-11</dcterms:issued> <dc:contributor>Rubenstein, Eric M.</dc:contributor> <dc:creator>Kreft, Stefan G.</dc:creator> <dc:contributor>Swanson, Robert</dc:contributor> <dc:creator>Swanson, Robert</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dcterms:title>Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase</dcterms:title> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-12-18T07:35:45Z</dcterms:available> <dcterms:abstract xml:lang="eng">Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD) in yeast, target distinct subsets of misfolded or otherwise abnormal proteins based primarily on degradation signal (degron) location. We report the surprising observation that fusing Deg1, a cytoplasmic degron normally recognized by Doa10, to the Sec62 membrane protein rendered the protein a Hrd1 substrate. Hrd1-dependent degradation occurred when Deg1-Sec62 aberrantly engaged the Sec61 translocon channel and underwent topological rearrangement. Mutations that prevent translocon engagement caused a reversion to Doa10-dependent degradation. Similarly, a variant of apolipoprotein B, a protein known to be cotranslocationally targeted for proteasomal degradation, was also a Hrd1 substrate. Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon.</dcterms:abstract> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-12-18T07:35:45Z</dc:date> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21018"/> <dc:contributor>Kreft, Stefan G.</dc:contributor> <dc:contributor>Greenblatt, Wesley</dc:contributor> <dc:creator>Hochstrasser, Mark</dc:creator> <dc:contributor>Hochstrasser, Mark</dc:contributor> <dc:creator>Greenblatt, Wesley</dc:creator> <dcterms:bibliographicCitation>Journal of Cell Biology ; 197 (2012), 6. - S. 761-773</dcterms:bibliographicCitation> <dc:language>eng</dc:language> <dc:creator>Rubenstein, Eric M.</dc:creator> <dc:rights>deposit-license</dc:rights> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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