ArticleProceedings of the National Academy of Sciences of the United States of America2004
A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 72 citations in OpenAlex.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Development of a fluorescence and quencher-based FRET assay for detection of endogenous peptide:N-glycanase/NGLY1 activity.The Journal of biological chemistry · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Comparative proteomics reveals elevated CCN2 in NGLY1-deficient cells.Biochemical and biophysical research communications · 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
- Article
- Orthopaedic phenotyping of NGLY1 deficiency using an international, family-led disease registry.Orphanet journal of rare diseases · 2019Article
- Article
- Limited ER quality control for GPI-anchored proteins.The Journal of cell biology · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- A congenital disorder of deglycosylation: Biochemical characterization of N-glycanase 1 deficiency in patient fibroblasts.Glycobiology · 2015Article
- Article
- Article
- Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum.BMC biochemistry · 2012Article
- Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.PloS one · 2012Article
- A ubiquitin independent degradation pathway utilized by a hepatitis B virus envelope protein to limit antigen presentation.PloS one · 2011Article
- 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
- Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.The Journal of biological chemistry · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Peptide:N-glycanase (PNGase) has been proposed to participate in the proteasome-dependent glycoprotein degradation pathway. The finding that yeast PNGase interacts with the 19S proteasome subunit through the protein Rad23 supports this hypothesis. In this report, we have used immunofluorescence, subcellular fractionation, coimmunoprecipitation, and in vitro GST pull-down techniques for detecting intracellular localization and interactions of PNGase, HR23B, and S4 by using human (h) and mouse (m) homologs. Immunofluorescence studies revealed that hPNGase, hHR23B, and hS4 are present in close proximity to the endoplasmic reticulum (ER) when calnexin was used as an ER marker in HeLa cells. Subcellular fractionation suggests not only cytoplasmic but also ER association of hPNGase in HeLa cells. Immunoprecipitation analysis revealed the interaction of h/mPNGase with the 19S proteasome subunit, hS4, through hHR23B. Using an in vitro GST pull-down assay, we also have shown that recombinant mPNGase requires its N terminus and middle domain for interaction with mHR23B. Finally, using misfolded yeast carboxypeptidase Y and chicken ovalbumin as glycoprotein substrates, we have established that mHR23B acts as a receptor for deglycosylated proteins. Based on this finding, we propose that after deglycosylation of misfolded glycoproteins by PNGase, the aglyco forms of these proteins are recognized by HR23B and targeted for degradation.
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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.