A membrane protein required for dislocation of misfolded proteins from the ER

By Brendan N Lilley, Hidde L. Ploegh. Nature, 2004

745 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Immunology

View Paper: https://www.semanticscholar.org/paper/e6b6aad454b6f6285816b4e711d29ef60d617b39

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Epidemiology

In Immunology

Citations in the corpus

In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “Sec61 (410, 411) and/or Der- lin1 and Derlin2 (228, 424) have been identified as potential components of proteinaceous channel(s) proposed to be used for retro-translocation of ERAD substrates from the ER lumen into the cytosol.”
Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. (2006, background): “, 2006) and Der1p (Lilley and Ploegh, 2004; Ye et al., 2004), a membrane protein that spans the membrane four times (Knop et al.”
AAA+ proteins: have engine, will work (2005, background): “, and has recently been shown to associate with the transmembrane protein Derlin, a candidate retrotranslocation channe”
One step at a time: endoplasmic reticulum-associated degradation (2008, background): “In line with this view, derlin-1, one of three derlin homologues in human cells, interacts with components of the ubiquitylation and targeting machinery, and partakes in the HCMV-catalysed turnover of MHC”
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol (2004, background): “First, US11 interacts with heavy chains in the ER lumen and targets them to Derlin-1, as is also reported in a parallel pape”
Quality control: ER-associated degradation: protein quality control and beyond. (2014, positive): “US11 uses its transmembrane domain to recruit MHC I into a complex which contains Derlin-1 as well as Sel1L, the p97 ATPase complex and its membrane adaptor UBXD8 (Lilley and Ploegh, 2004; Ye et al., 2004; Mueller et al., 2008).”
Cellular response to endoplasmic reticulum stress: a matter of life or death (2006, background): “Mammalian ERAD pathways are less well understood than those of yeast, but several parallels are clear.8,9 As in yeast, glycosylation probably participates in the recognition of mammalian ERAD substrates,73 as do BiP and PDI.74,75 Similarly, at least some mammalian ERAD substrates may be dislocated t”
ERAD: the long road to destruction (2005, background): “Another protein suggested to form an export channel in the ER is the mammalian protein Derlin-1 and its yeast homologue Der1”