Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/82239
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Type: Journal article
Title: SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production
Author: Friedmann, E.
Hauben, E.
Maylandt, K.
Schleeger, S.
Vreugde, S.
Lichtenthaler, S.
Kuhn, P.
Stauffer, D.
Rovelli, G.
Martoglio, B.
Citation: Nature Cell Biology, 2006; 8(8):849-854
Publisher: Nature Publishing Group
Issue Date: 2006
ISSN: 1465-7392
1476-4679
Statement of
Responsibility: 
Robert Gauss, Ernst Jarosch, Thomas Sommer and Christian Hirsch
Abstract: A quality-control system surveys the lumen of the endoplasmic reticulum for terminally misfolded proteins. Polypeptides singled out by this system are ultimately degraded by the cytosolic ubiquitin-proteasome pathway. Key components of both the endoplasmic reticulum quality-control system and the degradation machinery have been identified, but a connection between the two systems has remained elusive. Here, we report an association between the endoplasmic reticulum quality-control lectin Yos9p and Hrd3p, a component of the ubiquitin-proteasome system that links these pathways. We identify designated regions in the luminal domain of Hrd3p that interact with Yos9p and the ubiquitin ligase Hrd1p. Binding of misfolded proteins occurs through Hrd3p, suggesting that Hrd3p recognises proteins that deviate from their native conformation, whereas Yos9p ensures that only terminally misfolded polypeptides are degraded.
Rights: © 2006 Nature PublishingGroup
DOI: 10.1038/ncb1445
Appears in Collections:Aurora harvest
Surgery publications

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