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.
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.
D000199:Actins / Q000097:blood*; D001704:Biopolymers; D003572:Cytochalasins / Q000097:blood*; D003850:Deoxyribonuclease I; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013049:Spectrin / Q000378:metabolism*
D000199:Actins; D001704:Biopolymers; D003572:Cytochalasins; D013049:Spectrin; D003850:Deoxyribonuclease I