ArticleBiochemistry2006
Thermal stabilities of brain spectrin and the constituent repeats of subunits.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dystrophin As a Molecular Shock Absorber.ACS nano · 2018Article
- Fluorescence study of the effect of cholesterol on spectrin-aminophospholipid interactions.European biophysics journal : EBJ · 2015Article
- Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.Journal of fluorescence · 2015Article
- Spectrin tetramer formation is not required for viable development in Drosophila.The Journal of biological chemistry · 2015Article
- Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.PloS one · 2015Article
- Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.PloS one · 2013Article
- Structural organization of the nine spectrin repeats of Kalirin.Biochemistry · 2012Article
- Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study.Journal of biomolecular NMR · 2012Article
- Visualizing dynamic cytoplasmic forces with a compliance-matched FRET sensor.Journal of cell science · 2011Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Stabilization of the spectrin-like domains of nesprin-1α by the evolutionarily conserved "adaptive" domain.Cellular and molecular bioengineering · 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
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The different genes that encode mammalian spectrins give rise to proteins differing in their apparent stiffness. To explore this, we have compared the thermal stabilities of the structural repeats of brain spectrin subunits (alphaII and betaII) with those of erythrocyte spectrin (alphaI and betaI). The unfolding transition midpoints (T(m)) of the 36 alphaII- and betaII-spectrin repeats extend between 24 and 82 degrees C, with an average higher by some 10 degrees C than that of the alphaI- and betaI-spectrin repeats. This difference is reflected in the T(m) values of the intact brain and erythrocyte spectrins. Two of three tandem-repeat constructs from brain spectrin exhibited strong cooperative coupling, with elevation of the T(m) of the less stable partner corresponding to coupling free energies of approximately -4.4 and -3.5 kcal/mol. The third tandem-repeat construct, by contrast, exhibited negligible cooperativity. Tandem-repeat mutants, in which a part of the "linker" helix that connects the two domains was replaced with a corresponding helical segment from erythroid spectrin, showed only minor perturbation of the thermal melting profiles, without breakdown of cooperativity. Thus, the linker regions, which tolerate few point mutations without loss of cooperative function, have evidently evolved to permit conformational coupling in specified regions. The greater structural stability of the repeats in alphaII- and betaII-spectrin may account, at least in part, for the higher rigidity of brain compared to erythrocyte spectrin.
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