ArticleThe Journal of biological chemistry2013
Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 124 citations in OpenAlex.
- Article
- Enzyme Assemblies in Nucleotide Metabolism: Structure, Regulation, and Disease Implications.Advances in experimental medicine and biology · 2026Review
- Hemoglobin A1C: Intracellular Heterogeneity and Functional Implications in Prediabetic and T2 Diabetic Erythrocytes.International journal of molecular sciences · 2025Article
- Proteostasis and metabolic dysfunction characterize a subset of storage-induced senescent erythrocytes targeted for posttransfusion clearance.The Journal of clinical investigation · 2025Article
- Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An overview of hereditary spherocytosis and the curative effects of splenectomy.Frontiers in physiology · 2025Review
- Interplay Between Metabolic Pathways and Increased Oxidative Stress in Human Red Blood Cells.Cells · 2024Review
- Organization of a functional glycolytic metabolon on mitochondria for metabolic efficiency.Nature metabolism · 2024Article
- Impact of cold storage on the oxygenation and oxidation reactions of red blood cells.Frontiers in physiology · 2024Article
- Mitapivat reprograms the RBC metabolome and improves anemia in a mouse model of hereditary spherocytosis.JCI insight · 2023Article
- The Impact of CaCells · 2023Article
- The Reactive Species Interactome in Red Blood Cells: Oxidants, Antioxidants, and Molecular Targets.Antioxidants (Basel, Switzerland) · 2023Article
- The roles of molecular chaperones in regulating cell metabolism.FEBS letters · 2023Review
- Intracellular Phage Tail-Like Nanostructures Affect Susceptibility of Streptomyces lividans to Osmotic Stress.mSphere · 2023Article
- Article
- Redox proteomics combined with proximity labeling enables monitoring of localized cysteine oxidation in cells.Cell chemical biology · 2023Article
- Mechanisms underlying the anti-aging activity of bergamot (Frontiers in physiology · 2023Article
- Identification of ExportedMicroorganisms · 2022Article
- Metabolic evidence for distinct pyruvate pools inside plant mitochondria.Nature plants · 2022Article
- Circulating primitive murine erythroblasts undergo complex proteomic and metabolomic changes during terminal maturation.Blood advances · 2022Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Glycolytic enzymes (GEs) have been shown to exist in multienzyme complexes on the inner surface of the human erythrocyte membrane. Because no protein other than band 3 has been found to interact with GEs, and because several GEs do not bind band 3, we decided to identify the additional membrane proteins that serve as docking sites for GE on the membrane. For this purpose, a method known as "label transfer" that employs a photoactivatable trifunctional cross-linking reagent to deliver a biotin from a derivatized GE to its binding partner on the membrane was used. Mass spectrometry analysis of membrane proteins that were biotinylated following rebinding and photoactivation of labeled GAPDH, aldolase, lactate dehydrogenase, and pyruvate kinase revealed not only the anticipated binding partner, band 3, but also the association of GEs with specific peptides in α- and β-spectrin, ankyrin, actin, p55, and protein 4.2. More importantly, the labeled GEs were also found to transfer biotin to other GEs in the complex, demonstrating for the first time that GEs also associate with each other in their membrane complexes. Surprisingly, a new GE binding site was repeatedly identified near the junction of the membrane-spanning and cytoplasmic domains of band 3, and this binding site was confirmed by direct binding studies. These results not only identify new components of the membrane-associated GE complexes but also provide molecular details on the specific peptides that form the interfacial contacts within each interaction.
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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.