Identification and Location of Brain Protein 4.1
- 29 June 1984
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 224 (4656), 1433-1436
- https://doi.org/10.1126/science.6374897
Abstract
Protein 4.1 is a membrane skeletal protein that converts the low-affinity interaction between spectrin and actin into a high-affinity ternary complex of spectrin, protein 4.1, and actin that is essential to the structural stability of the erythrocyte. Pig brain was shown to contain an 87-kilodalton immunoreactive analog of protein 4.1 that has partial sequence homology with pig erythrocyte protein 4.1 and the same location as spectrin in the cortical cytoplasm of neuronal and glial cell types of the cerebellum.This publication has 26 references indexed in Scilit:
- Properties of brain spectrin (fodrin)FEBS Letters, 1983
- Complexes containing actin and spectrin from erythrocyte and brainCell Motility, 1983
- A Genetic Defect in the Binding of Protein 4.1 to Spectrin in a Kindred with Hereditary SpherocytosisNew England Journal of Medicine, 1982
- Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell typesThe Journal of cell biology, 1982
- A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cellsNature, 1982
- Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrinNature, 1982
- Widespread occurrence of avian spectrin in nonerythroid cellsCell, 1982
- Purification of a 240 000 Mr calmodulin‐binding protein from a microsomal fraction of brainFEBS Letters, 1981
- Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability.Journal of Clinical Investigation, 1981
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971