ArticleMolecular biology of the cell2005
The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 78 citations in OpenAlex.
- Natural SEL1L variants rescue a model of NGLY1 deficiency and modify ERAD function and proteasome sensitivity.PLoS genetics · 2025Article
- An in vivo drug repurposing screen and transcriptional analyses reveals the serotonin pathway and GSK3 as major therapeutic targets for NGLY1 deficiency.PLoS genetics · 2022Article
- Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation.Nutrients · 2022Review
- NGLY1 Deficiency, a Congenital Disorder of Deglycosylation: From Disease Gene Function to Pathophysiology.Cells · 2022Review
- AeLife · 2020Article
- Human genome-wide RNAi screen reveals host factors required for enterovirus 71 replication.Nature communications · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Glycoprotein Quality Control and Endoplasmic Reticulum Stress.Molecules (Basel, Switzerland) · 2015Review
- Article
- The mammalian endoplasmic reticulum-associated degradation system.Cold Spring Harbor perspectives in biology · 2013Review
- Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum.BMC biochemistry · 2012Article
- Derlin-1 and UBXD8 are engaged in dislocation and degradation of lipidated ApoB-100 at lipid droplets.Molecular biology of the cell · 2012Article
- Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.The Journal of biological chemistry · 2011Article
- Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Cell research · 2011Review
- A new autophagy-related checkpoint in the degradation of an ERAD-M target.The Journal of biological chemistry · 2011Article
- Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps.The Journal of biological chemistry · 2011Article
- Protective unfolded protein response in human pancreatic beta cells transplanted into mice.PloS one · 2010Article
- Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster.PloS one · 2010Article
- The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Identification of miR-21 targets in breast cancer cells using a quantitative proteomic approach.Proteomics · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The deglycosylating enzyme, peptide:N-glycanase, acts on misfolded N-linked glycoproteins dislocated from the endoplasmic reticulum (ER) to the cytosol. Deglycosylation has been demonstrated to occur at the ER membrane and in the cytosol. However, the mechanism of PNGase association with the ER membrane was unclear, because PNGase lacked the necessary signal to facilitate its incorporation in the ER membrane, nor was it known to bind to an integral ER protein. Using HeLa cells, we have identified a membrane protein that associates with PNGase, thereby bringing it in close proximity to the ER and providing accessibility to dislocating glycoproteins. This protein, Derlin-1, has recently been shown to mediate retrotranslocation of misfolded glycoproteins. In this study we demonstrate that Derlin-1 interacts with the N-terminal domain of PNGase via its cytosolic C-terminus. Moreover, we find PNGase distributed in two populations; ER-associated and free in the cytosol, which suggests the deglycosylation process can proceed at either site depending on the glycoprotein substrate.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.