Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
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چکیده
منابع مشابه
Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions
The ability of protein 4.1 to stimulate the binding of spectrin to F-actin has been compared by cosedimentation analysis for three avian (erythrocyte, brain, and brush border) and two mammalian (erythrocyte and brain) spectrin isoforms. Human erythroid protein 4.1 stimulated actin binding of all spectrins except the brush border isoform (TW 260/240). These results suggested that the beta subuni...
متن کاملInteractions of the alpha-spectrin N-terminal region with beta-spectrin. Implications for the spectrin tetramerization reaction.
Spectrin of the erythrocyte membrane skeleton is composed of alpha- and beta-spectrin, which associate to form heterodimers and tetramers. It has been suggested that a fractional domain (helix C) in the amino-terminal region of alpha-spectrin (Nalpha region) bundles with another fractional domain in the carboxyl-terminal region of beta-spectrin (Cbeta region) to yield a triple alpha-helical bun...
متن کاملInteractions of spectrin in hereditary elliptocytes containing truncated spectrin beta-chains.
An abnormal spectrin, in which one subunit is truncated, has been detected in a large German family. The inheritance is autosomal dominant. The affected members of the family suffer in widely varying degree from a microcytic hemolytic anemia. The red cell morphology varies correspondingly from smooth elliptocytes to predominantly poikilocytes. The abnormal spectrin makes up approximately 30% of...
متن کاملThe carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding.
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 domai...
متن کاملThe carboxyterminal EF domain of erythroid -spectrin is necessary for optimal spectrin-actin binding
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1987
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.104.3.519