ArticleThe Biochemical journal1998
Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Development of Mechanical Stability in Late-Stage Embryonic Erythroid Cells: Insights From Fluorescence Imaged Micro-Deformation Studies.Frontiers in physiology · 2021Article
- Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats.Protein science : a publication of the Protein Society · 2019Article
- Genotype-phenotype correlations in hereditary elliptocytosis and hereditary pyropoikilocytosis.Blood cells, molecules & diseases · 2016Article
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Biophysical journal · 2012Article
- Recessive mutations in SPTBN2 implicate β-III spectrin in both cognitive and motor development.PLoS genetics · 2012Article
- Article
- Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs.Protein science : a publication of the Protein Society · 2011Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.Blood · 2010Article
- Association studies of erythroid alpha-spectrin at the tetramerization site.British journal of haematology · 2009Article
- Conformational changes at the tetramerization site of erythroid alpha-spectrin upon binding beta-spectrin: a spin label EPR study.Biochemistry · 2008Article
- Article
- Article
- Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway.The Journal of cell biology · 2006Article
- The transitional junction: a new functional subcellular domain at the intercalated disc.Molecular biology of the cell · 2006Article
- Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site.The Biochemical journal · 2003Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most of hereditary elliptocytosis (HE) cases are related to a spectrin dimer (SpD) self-association defect. The severity of haemolysis is correlated with the extent of the SpD self-association defect, which itself depends on the location of the mutation regarding the tetramerization site. This site is presumed to involve the first C helix of the alpha chain and the last two helices, A and B, of the beta chain to reconstitute a triple helical structure (A, B and C), as observed along spectrin. Using recombinant peptides, we demonstrated that the first C helix of the alpha chain and the last two helices of the beta chain alone are not sufficient to establish interactions, which only occurred when a complete triple-helical repeat was added to each partner. One adjacent repeat is necessary to stabilize the conformation of both N- and C-terminal structures directly involved in the interaction site and is sufficient to generate a binding affinity similar to that observed in the native molecule. Producing peptides carrying a betaHE mutation, we reproduced the tetramerization defect as observed in patients. Therefore, the betaW2024R and betaW2061R mutations, which replace the invariant tryptophan and a residue located in the hydrophobic core, respectively, affect alpha-beta interactions considerably. In contrast, the betaA2013V mutation, which modifies a residue located outside any presumed interacting regions, has a minor effect on the interaction.
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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.