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Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin

, : Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin. Journal of Biological Chemistry 254(17): 8620-8627

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Accession: 041409022

PMID: 468843

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Related references

Brenner S.L.; Korn E.D., 1979: Spectrin tetramer cross links f actin. Federation Proceedings 38(3 PART 1): 469

Fishkind, D.J.; Bonder, E.M.; Begg, D.A., 1987: Isolation and characterization of sea urchin egg spectrin: calcium modulation of the spectrin-actin interaction. Sea urchin egg spectrin has been purified from a homogenate of unfertilized Strongylocentrotus purpuratus eggs using standard biochemical procedures. SDS-PAGE analysis of the molecule revealed a closely spaced, high molecular weight doublet at 237...

Fowler, V.; Taylor, D.L., 1980: Spectrin plus band 4.1 cross-link actin. Regulation by micromolar calcium. A low-salt extract prepared from human erythrocyte membranes forms a solid gel when purified rabbit muscle G- or F-actin is added to it to give a concentration of approximately 1 mg/ml. This extract contains spectrin, actin, band 4.1, band 4.9, he...

Husain, A.; Sawyer, W.H.; Howlett, G.J., 1983: The effect of cross-linking spectrin-actin complexes with band 4.1 on the state of polymerization of the actin. The polymerization of actin in the presence of spectrin tetramers and band 4.1 isolated from the human erythrocyte has been measured using a fluorescence energy transfer technique. The results show that the cross-linking of spectrin-actin complexe...

Li, D.; Harper, S.L.; Tang, H-Yao.; Maksimova, Y.; Gallagher, P.G.; Speicher, D.W., 2010: A comprehensive model of the spectrin divalent tetramer binding region deduced using homology modeling and chemical cross-linking of a mini-spectrin. Spectrin dimer-tetramer interconversion is a critical contributor to red cell membrane stability, but some properties of spectrin tetramer formation cannot be studied effectively using monomeric recombinant domains. To address these limitations, a...

Korn E.D., 1979: Acceleration of actin polymerization by spectrin actin complex and inhibition by cytochalasin evidence for an f actin treadmill. Journal Of Cell Biologypart 2: 311a

Korsgren, C.; Lux, S.E., 2010: The 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...

Tomaselli M.B.; Lux S.E., 1977: Elliptical spectrin actin skeletons and heat sensitive spectrin in hereditary elliptocytosis. Clinical Research 25(3): 519A

Coleman, T.R.; Harris, A.S.; Mische, S.M.; Mooseker, M.S.; Morrow, J.S., 1987: 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 eryt...

Cohen C.M.; Foley S.F., 1980: Spectrin dependent and spectrin independent association of f actin with the erythrocyte membrane. Binding of F-actin to spectrin-actin-depleted [human] erythrocyte membrane inside-out vesicles was measured using [3H]F-actin. F-actin binding to vesicles at C was stimulated 5- to 10-fold by addition of spectrin dimers or tetramers to...