spectrin
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Function
- interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for regulation of plasma membrane components & for maintenance of lipid asymmetry of the plasma membrane
- spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane
- associates with band 4.1 & actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane
- F-actin pointed end capping protein
- also F-actin bundling protein
Structure
- composed of nonhomologous chains, spectrin-alpha & spectrin-beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, & higher polymers
Compartment
- complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin & mediates the binding of the whole complex to a transmembrane protein band 3
Pathology
- spectrin deficiency associated with hereditary spherocytosis
More general terms
- blood protein
- membrane protein
- cytoskeletal protein
- calmodulin binding protein
- PEST protein
- multisubunit protein
Additional terms
References
- ↑ Cantley LC, Auger KR, Carpenter C, Duckworth B, Graziani A, Kapeller R, Soltoff S. Oncogenes and signal transduction. Cell. 1991 Jan 25;64(2):281-302. Review. Erratum in: Cell 1991 May 31;65(5):following 914. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1846320