ArticleBiochemistry2008
Molecular epitopes of the ankyrin-spectrin interaction.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Ankyrin-G and Its Binding Partners in Neurons: Orchestrating the Molecular Structure of the Axon Initial Segment.Biomolecules · 2025Review
- Spherocytosis-Related L1340P Mutation in Ankyrin Affects Its Interactions with Spectrin.Life (Basel, Switzerland) · 2023Article
- Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020Review
- Plug-and-Play Protein Modification Using Homology-Independent Universal Genome Engineering.Neuron · 2019Article
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- The Plasmodium falciparum exported protein PF3D7_0402000 binds to erythrocyte ankyrin and band 4.1.Molecular and biochemical parasitology · 2017Article
- An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates.Analytical biochemistry · 2016Article
- Interaction of Plasmodium vivax Tryptophan-rich Antigen PvTRAg38 with Band 3 on Human Erythrocyte Surface Facilitates Parasite Growth.The Journal of biological chemistry · 2015Article
- β-III spectrin underpins ankyrin R function in Purkinje cell dendritic trees: protein complex critical for sodium channel activity is impaired by SCA5-associated mutations.Human molecular genetics · 2014Article
- Identification of cytoskeletal elements enclosing the ATP pools that fuel human red blood cell membrane cation pumps.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structurally similar but functionally diverse ZU5 domains in human erythrocyte ankyrin.Journal of molecular biology · 2012Article
- Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Recessive mutations in SPTBN2 implicate β-III spectrin in both cognitive and motor development.PLoS genetics · 2012Article
- Erythrocyte membrane changes of chorea-acanthocytosis are the result of altered Lyn kinase activity.Blood · 2011Article
- Do we already know how spectrin attracts ankyrin?Cellular and molecular life sciences : CMLS · 2010Review
- Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage.Biochemistry · 2010Article
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- Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of beta-spectrin.Biochemical and biophysical research communications · 2010Article
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Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Isoforms of ankyrin and its binding partner spectrin are responsible for a number of interactions in a variety of human cells. Conflicting evidence, however, had identified two different, non-overlapping human erythroid ankyrin subdomains, Zu5 and 272, as the minimum binding region for beta-spectrin. Complementary studies on the ankyrin-binding domain of spectrin have been somewhat more conclusive yet have not presented binding in terms of well-phased, integral numbers of spectrin repeats. Thus, the objective of this study was to clearly define and characterize the minimal ankyrin-spectrin binding epitopes. Circular dichroism (CD) wavelength spectra of the aforementioned ankyrin subdomains show that these fragments are 30-60% unstructured. In contrast, human erythroid beta-spectrin repeats 13, 14, 15, and 16 (prepared in all combinations of two adjacent repeats) demonstrated proper folding and stability as determined by CD and tryptophan wavelength and heat denaturation scans. Native polyacrylamide gel electrophoresis (PAGE) gel shifts as well as affinity pull-down assays implicated Zu5 and beta-spectrin repeats 14-15 as the minimum binding epitopes. These results were confirmed by analytical ultracentrifugation to sedimentation equilibrium by which a 1:1 complex was obtained if and only if Zu5 was mixed with beta-spectrin constructs containing repeats 14 and 15 in tandem. Surface plasmon resonance yielded a K D of 15.2 nM for binding of beta-spectrin fragments to the ankyrin subdomain Zu5, accounting for all of the binding observed between the intact molecules. Collectively, these results show the 14th and 15th beta-spectrin repeats comprise the minimal, phased region of beta-spectrin, which binds ankyrin at the Zu5 subdomain with high affinity.
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