ArticlePloS one2012
Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- The RAGE Axis: A Relevant Inflammatory Hub in Human Diseases.Biomolecules · 2024Review
- S100B actions on glial and neuronal cells in the developing brain: an overview.Frontiers in neuroscience · 2024Review
- Article
- Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy.Biochimica et biophysica acta. Molecular basis of disease · 2023Article
- The Remarkable Roles of the Receptor for Advanced Glycation End Products (RAGE) and Its Soluble Isoforms in COVID-19: The Importance of RAGE Pathway in the Lung Injuries.Indian journal of clinical biochemistry : IJCB · 2023Review
- Role and Therapeutic Potential of RAGE Signaling in Neurodegeneration.Current drug targets · 2022Article
- Molecular Characteristics of RAGE and Advances in Small-Molecule Inhibitors.International journal of molecular sciences · 2021Review
- RAGE Signaling in Melanoma Tumors.International journal of molecular sciences · 2020Review
- Insights Into the Mechanism of MCT8 Oligomerization.Journal of the Endocrine Society · 2020Article
- Enhanced oligomerization of full-length RAGE by synergy of the interaction of its domains.Scientific reports · 2019Article
- Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology.International journal of molecular sciences · 2019Review
- Molecular and antigenic characterization of Trypanosoma cruzi TolT proteins.PLoS neglected tropical diseases · 2019Article
- Advanced Glycation End Products Stimulate Angiotensinogen Production in Renal Proximal Tubular Cells.The American journal of the medical sciences · 2019Article
- Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures.Medicines (Basel, Switzerland) · 2018Article
- Change in the Molecular Dimension of a RAGE-Ligand Complex Triggers RAGE Signaling.Structure (London, England : 1993) · 2016Article
- Regulation of Receptor for Advanced Glycation End Products (RAGE) Ectodomain Shedding and Its Role in Cell Function.The Journal of biological chemistry · 2016Article
- GeneOptimizer program-assisted cDNA reengineering enhances sRAGE autologous expression in Chinese hamster ovary cells.Protein expression and purification · 2014Article
- The N-glycoform of sRAGE is the key determinant for its therapeutic efficacy to attenuate injury-elicited arterial inflammation and neointimal growth.Journal of molecular medicine (Berlin, Germany) · 2013Article
- Alternative splicing of the RAGE cytoplasmic domain regulates cell signaling and function.PloS one · 2013Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe receptor for advanced glycation end products (RAGE) on the cell surface transmits inflammatory signals. A member of the immunoglobulin superfamily, RAGE possesses the V, C1, and C2 ectodomains that collectively constitute the receptor's extracellular structure. However, the molecular mechanism of RAGE biogenesis remains unclear, impeding efforts to control RAGE signaling through cellular regulation. METHODOLOGY AND
resultWe used co-immunoprecipitation and crossing-linking to study RAGE oligomerization and found that RAGE forms dimer-based oligomers. Via non-reducing SDS-polyacrylamide gel electrophoresis and mutagenesis, we found that cysteines 259 and 301 within the C2 domain form intermolecular disulfide bonds. Using a modified tripartite split GFP complementation strategy and confocal microscopy, we also found that RAGE dimerization occurs in the endoplasmic reticulum (ER), and that RAGE mutant molecules without the double disulfide bridges are unstable, and are subjected to the ER-associated degradation.
conclusionDisulfide bond-mediated RAGE dimerization in the ER is the critical step of RAGE biogenesis. Without formation of intermolecular disulfide bonds in the C2 region, RAGE fails to reach cell surface. SIGNIFICANCE: This is the first report of RAGE intermolecular disulfide bond.
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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.