A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

By Y. Ye, Y. Shibata, Chi Y. Yun, D. Ron, Tom A. Rapoport. Nature, 2004

1,034 citations recorded by the source corpus.

Subfields: Aging, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/07a04ec4a979acbf67ef9b08fe4b4bc8098232b8

How researchers see this paper

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

In Aging

In Cell Biology

In Molecular Biology

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.”
A class of membrane proteins shaping the tubular endoplasmic reticulum. (2006, neutral): “described previously (Dreier and Rapoport, 2000; Ye et al., 2004).”
A membrane protein required for dislocation of misfolded proteins from the ER (2004, methodology): “used a different approach and have reached a similar conclusio”
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.”
Endoplasmic reticulum stress signaling in disease. (2006, background): “Some evidence supports a role for the original Sec61 translocon complex (150, 228), although a new complex containing derlin-1 and p97, a cytosolic ATPase, has been shown to be involved in retrotranslocation of major histocompatibility complex (MHC) class I molecules (106, 219).”
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”
Protein quality control in the early secretory pathway (2008, background): “It remains to be seen whether derlins directly mediate dislocation, or act by recruiting additional essential components such as the AAA-ATPase p97, which provides part of the energy neces- sary for this step (Ye et al, 2001, 2004; Rabinovich et al, 2002; Oda et al, 2006).”
Selenium, Selenoproteins, and Immunity (2018, background): “Selenoprotein S SELENOS, SELS, SEPS1, VIMP Transmembrane protein found in ER involved in ER associated degradation [49,50].”
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”
Selenoproteins: molecular pathways and physiological roles. (2014, background): “SelS differs from SelK by the presence of an additional coiled-coil domain in the cytosolic portion of the protein, which has been proposed to mediate the interaction with other proteins or oligomerization of SelS (377).”
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”