ArticleBiochemistry2012
Identification of contact sites between ankyrin and band 3 in the human erythrocyte membrane.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- Subcellular Mechanical Imaging of Erythrocytes with Optically Correlated Scanning Ion Conductance Microscopy.ACS measurement science au · 2025Article
- Pleiotropic Ankyrins: Scaffolds for Ion Channels and Transporters.Channels (Austin, Tex.) · 2022Review
- Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane.Nature structural & molecular biology · 2022Article
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- The Role of RBC Oxidative Stress in Sickle Cell Disease: From the Molecular Basis to Pathologic Implications.Antioxidants (Basel, Switzerland) · 2021Review
- Comparison of pathological clotting using haematological, functional and morphological investigations in HIV-positive and HIV-negative patients with deep vein thrombosis.Retrovirology · 2020Article
- Oxidative Stress and Thrombosis during Aging: The Roles of Oxidative Stress in RBCs in Venous Thrombosis.International journal of molecular sciences · 2020Review
- Proeryptotic Activity of 4-Hydroxynonenal: A New Potential Physiopathological Role for Lipid Peroxidation Products.Biomolecules · 2020Article
- Molecular Simulations of Intact Anion Exchanger 1 Reveal Specific Domain and Lipid Interactions.Biophysical journal · 2019Article
- TRPA1-FGFR2 binding event is a regulatory oncogenic driver modulated by miRNA-142-3p.Nature communications · 2017Article
- Article
- Stomatin modulates the activity of the Anion Exchanger 1 (AE1, SLC4A1).Scientific reports · 2017Article
- Full-Length Anion Exchanger 1 Structure and Interactions with Ankyrin-1 Determined by Zero Length Crosslinking of Erythrocyte Membranes.Structure (London, England : 1993) · 2017Article
- Article
- A novel ENU-induced ankyrin-1 mutation impairs parasite invasion and increases erythrocyte clearance during malaria infection in mice.Scientific reports · 2016Article
- Identification of adducin-binding residues on the cytoplasmic domain of erythrocyte membrane protein, band 3.The Biochemical journal · 2016Article
- A novel strain energy relationship for red blood cell membrane skeleton based on spectrin stiffness and its application to micropipette deformation.Biomechanics and modeling in mechanobiology · 2016Article
- The Effect of Polymeric Nanoparticles on Biocompatibility of Carrier Red Blood Cells.PloS one · 2016Article
- Evidence of a structural and functional ammonium transporter RhBG·anion exchanger 1·ankyrin-G complex in kidney epithelial cells.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The red cell membrane is stabilized by a spectrin/actin-based cortical cytoskeleton connected to the phospholipid bilayer via multiple protein bridges. By virtue of its interaction with ankyrin and adducin, the anion transporter, band 3 (AE1), contributes prominently to these bridges. In a previous study, we demonstrated that an exposed loop comprising residues 175-185 of the cytoplasmic domain of band 3 (cdB3) constitutes a critical docking site for ankyrin on band 3. In this paper, we demonstrate that an adjacent loop, comprising residues 63-73 of cdB3, is also essential for ankyrin binding. Data that support this hypothesis include the following. (1) Deletion or mutation of residues within the latter loop abrogates ankyrin binding without affecting cdB3 structure or its other functions. (2) Association of cdB3 with ankyrin is inhibited by competition with the loop peptide. (3) Resealing of the loop peptide into erythrocyte ghosts alters membrane morphology and stability. To characterize cdB3-ankyrin interaction further, we identified their interfacial contact sites using molecular docking software and the crystal structures of D(3)D(4)-ankyrin and cdB3. The best fit for the interaction reveals multiple salt bridges and hydrophobic contacts between the two proteins. The most important ion pair interactions are (i) cdB3 K69-ankyrin E645, (ii) cdB3 E72-ankyrin K611, and (iii) cdB3 D183-ankyrin N601 and Q634. Mutation of these four residues on ankyrin yielded an ankyrin with a native CD spectrum but little or no affinity for cdB3. These data define the docking interface between cdB3 and ankyrin in greater detail.
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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.