Spectrin-4.1-actin complex of the human erythrocyte: molecular basis of its ability to bind cytochalasins with high-affinity and to accelerate actin polymerization in vitro

Journal of Supramolecular Structure and Cellular Biochemistry
D C Lin

Abstract

The spectrin-4.1-actin complex isolated from the cytoskeleton of human erythrocyte was found to be similar to muscle F-actin in several aspects: Both the complex and F-actin nucleate cytochalasin-sensitive actin polymerization; both bind dihydrocytochalasin B with similar binding contrasts; both can be depolymerized by DNase I with loss of cytochalasin binding activity. From these results, we conclude that the actin in the complex is in an oligomeric form. However, the presence of spectrin and band 4.1 in the complex not only stabilized the actin in the complex as evidenced by its resistance to depolymerization in low-ionic-strength conditions and to DNase I as compared with F-actin, but also altered the characteristics of the binding site(s) for cytochalasins believed to be located at the "barbed" (polymerizing) end of the oligomeric actin.

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Citations

Mar 1, 1987·The Journal of Cell Biology·S C LiuJ Palek
Mar 1, 1983·The Journal of Cell Biology·J C Pinder, W B Gratzer
Jul 1, 1984·The Journal of Cell Biology·L G Tilney, M S Tilney
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Apr 21, 2007·Health & Social Care in the Community·Rafiqul I ChowdhuryNitai Chakraborty
Mar 30, 2010·Tropical Medicine & International Health : TM & IH·Merrin E RutherfordPhilip C Hill
Aug 31, 2006·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Gisela TünnemannM Cristina Cardoso
Nov 4, 1982·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·S LinD C Lin

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