ArticleProceedings of the National Academy of Sciences of the United States of America2006
Mammalian alpha I-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. 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, 43 citations in OpenAlex.
- Red cell shape regulation by band 3-ankyrin-spectrin linkage: implications for clinical severity of bovine hereditary spherocytosis.Blood red cells & iron · 2025Article
- αI-spectrin represents evolutionary optimization of spectrin for red blood cell deformability.Biophysical journal · 2021Article
- Extracellular Vesicles from Red Blood Cells and Their Evolving Roles in Health, Coagulopathy and Therapy.International journal of molecular sciences · 2020Review
- Defining new mechanistic roles for αII spectrin in cardiac function.The Journal of biological chemistry · 2019Article
- Image-based model of the spectrin cytoskeleton for red blood cell simulation.PLoS computational biology · 2017Article
- α-Spectrin and integrins act together to regulate actomyosin and columnarization, and to maintain a monolayered follicular epithelium.Development (Cambridge, England) · 2016Article
- Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs.Cell host & microbe · 2015Article
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Erythrocyte stiffness during morphological remodeling induced by carbon ion radiation.PloS one · 2014Article
- Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Biophysical journal · 2012Article
- Spectrin-based skeleton as an actor in cell signaling.Cellular and molecular life sciences : CMLS · 2012Review
- Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage.Biochemistry · 2010Article
- The dimensions and composition of stereociliary rootlets in mammalian cochlear hair cells: comparison between high- and low-frequency cells and evidence for a connection to the lateral membrane.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Article
- Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeleton.The Journal of biological chemistry · 2008Article
- Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.Protein science : a publication of the Protein Society · 2007Article
- Article
- Functional links between membrane transport and the spectrin cytoskeleton.The Journal of membrane biology · 2006Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Mammalian red blood cells, unlike those of other vertebrates, must withstand the rigors of circulation in the absence of new protein synthesis. Key to this is plasma membrane elasticity deriving from the protein spectrin, which forms a network on the cytoplasmic face. Spectrin is a tetramer (alphabeta)(2), made up of alphabeta dimers linked head to head. We show here that one component of erythrocyte spectrin, alphaI, is encoded by a gene unique to mammals. Phylogenetic analysis suggests that the other alpha-spectrin gene (alphaII) common to all vertebrates was duplicated after the emergence of amphibia, and that the resulting alphaI gene was preserved only in mammals. The activities of alphaI and alphaII spectrins differ in the context of the human red cell membrane. An alphaI-spectrin fragment containing the site of head-to-head interaction with the beta-chain binds more weakly than the corresponding alphaII fragment to this site. The latter competes so strongly with endogenous alphaI as to cause destabilization of membranes at 100-fold lower concentration than the alphaI fragment. The efficacies of alphaI/alphaII chimeras indicate that the partial structural repeat, which binds to the complementary beta-spectrin element, and the adjacent complete repeat together determine the strength of the dimer-dimer interaction on the membrane. Alignment of all available alpha-spectrin N-terminal sequences reveals three blocks of sequence unique to alphaI. Furthermore, human alphaII-spectrin is closer to fruitfly alpha-spectrin than to human alphaI-spectrin, consistent with adaptation of alphaI to new functions. We conclude that alphaI-spectrin represents a neofunctionalized spectrin adapted to the rapid make and break of tetramers.
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Registered trials
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