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 complexes by band 4.1 results in a limited depolymerization of actin filaments and a concomitant rise in the critical actin concentration. The phenomenon may explain in part the existence of actin in the erythrocyte cytoskeleton as short oligomers rather than as long filaments.
D000199:Actins / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D009479:Neuropeptides; D013049:Spectrin / Q000378:metabolism*; D013997:Time Factors
D000199:Actins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin