In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte.
The formation of a high-molecular weight complex between spectrin and F-actin depends on the presence of a third cytoskeletal constituent, protein 4.1. Electron microscopy shows that in this ternary complex the actin filaments are linked by bridges, which have the appearance of spectrin. The spectrin must be in the tetrameric state for such bridges to form: the dimer is evidently univalent, for it binds but forms no cross-links. G-actin also fails to form extended complexes. It is inferred that in the native cytoskeleton the spectrin is tetrameric and associated with 4.1 and probably oligomers of actin.
D000199:Actins / Q000378:metabolism*; D002474:Cell-Free System; D004910:Erythrocyte Membrane / Q000648:ultrastructure; D004912:Erythrocytes / Q000648:ultrastructure*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood / Q000378:metabolism*; D008970:Molecular Weight; D011485:Protein Binding; D013049:Spectrin / Q000378:metabolism*
D000199:Actins; D008565:Membrane Proteins; D013049:Spectrin