ArticleThe Biochemical journal2003
Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
- To deform or not to deform: the evolutionary basis of mammalian red blood cell deformability.Biophysical journal · 2021Article
- αI-spectrin represents evolutionary optimization of spectrin for red blood cell deformability.Biophysical journal · 2021Article
- Pathogenic SPTBN1 variants cause an autosomal dominant neurodevelopmental syndrome.Nature genetics · 2021Article
- Novel variants in SPTAN1 without epilepsy: An expansion of the phenotype.American journal of medical genetics. Part A · 2018Article
- Comparison of prognoses according to non-positive and positive spectrin αII expression detected immunohistochemically in epithelial ovarian carcinoma: a retrospective study.Cancer medicine · 2016Article
- Spectrin tetramer formation is not required for viable development in Drosophila.The Journal of biological chemistry · 2015Article
- Mechanical control of the sense of touch by β-spectrin.Nature cell biology · 2014Article
- 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
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- 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
- Cardiac spectrins: alternative splicing encodes functional diversity.Journal of molecular and cellular cardiology · 2010Article
- Characterization and expression of a heart-selective alternatively spliced variant of alpha II-spectrin, cardi+, during development in the rat.Journal of molecular and cellular cardiology · 2010Article
- Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation.The Journal of biological chemistry · 2010Article
- Association studies of erythroid alpha-spectrin at the tetramerization site.British journal of haematology · 2009Article
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- Article
- Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.Protein science : a publication of the Protein Society · 2007Article
- A search engine to identify pathway genes from expression data on multiple organisms.BMC systems biology · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Spectrin tetramers form by the interaction of two alpha-beta dimers through two helices close to the C-terminus of a beta subunit and a single helix at the N-terminus of an alpha subunit. Early work on spectrin from solid tissues (typified by alphaII and betaII polypeptides) indicated that it forms a more stable tetramer than erythroid spectrin (alphaI-betaI). In the present study, we have probed the molecular basis of this phenomenon. We have quantified the interactions of N-terminal regions of two human alpha polypeptides (alphaI and alphaII) with the C-terminal regions of three beta isoforms (betaISigma1, betaIISigma1 and betaIISigma2). alphaII binds either betaII form with a much higher affinity than alphaI binds betaISigma1 ( K (d) values of 5-9 nM and 840 nM respectively at 25 degrees C). betaIISigma1 and betaIISigma2 are splice variants with different C-terminal extensions outside the tetramerization site: these extensions affect the rate rather than the affinity of alpha subunit interaction. alphaII spectrin interacts with each beta subunit with higher affinity than alphaI, and the betaII polypeptides have higher affinities for both alpha chains than betaISigma1. The first full repeat of the alpha subunit has a major role in determining affinity. Enthalpy changes in the alphaII-betaIISigma2 interaction are large, but the entropy change is comparatively small. The interaction is substantially reduced, but not eliminated, by concentrated salt solutions. The high affinity and slow overall kinetics of association and dissociation of alphaII-betaII spectrin may suit it well to a role in strengthening cell junctions and providing stable anchor points for transmembrane proteins at points specified by cell-adhesion molecules.
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