ArticleBlood2010
The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding.
Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- The membrane skeleton is constitutively remodeled in neurons by calcium signaling.Science (New York, N.Y.) · 2025Article
- Paralemmin-1 controls the nanoarchitecture of the neuronal submembrane cytoskeleton.Science advances · 2025Article
- Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure and calcium-binding studies of calmodulin-like domain of human non-muscle α-actinin-1.Scientific reports · 2016Article
- Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes.Structure (London, England : 1993) · 2015Article
- Article
- Genetic studies of spectrin in the larval fat body of Drosophila melanogaster: evidence for a novel lipid uptake apparatus.Genetics · 2013Article
- Spectraplakins: master orchestrators of cytoskeletal dynamics.The Journal of cell biology · 2012Review
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Spectrin and protein 4.1R crosslink F-actin, forming the membrane skeleton. Actin and 4.1R bind to one end of β-spectrin. The adjacent end of α-spectrin, called the EF domain, is calmodulin-like, with calcium-dependent and calcium-independent EF hands. The severely anemic sph(1J)/sph(1J) mouse has very fragile red cells and lacks the last 13 amino acids in the EF domain, implying that the domain is critical for skeletal integrity. To test this, we constructed a minispectrin heterodimer from the actin-binding domain, the EF domain, and 4 adjacent spectrin repeats in each chain. The minispectrin bound to F-actin in the presence of native human protein 4.1R. Formation of the spectrin-actin-4.1R complex was markedly attenuated when the minispectrin contained the shortened sph(1J) α-spectrin. The α-spectrin deletion did not interfere with spectrin heterodimer assembly or 4.1R binding but abolished the binary interaction between spectrin and F-actin. The data show that the α-spectrin EF domain greatly amplifies the function of the β-spectrin actin-binding domain (ABD) in forming the spectrin-actin-4.1R complex. A model, based on the structure of α-actinin, suggests that the EF domain modulates the function of the ABD and that the C-terminal EF hands (EF(34)) may bind to the linker that connects the ABD to the first spectrin repeat.
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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.