Calspectin (fodrin or nonerythroid spectrin)-actin interaction: a possible involvement of 4.1-related protein.
The calspectin/actin complex extracted from the bovine brain membrane crosslinks F-actin, resulting in the increasing viscosity of F-actin determined by low-shear viscometry. We demonstrated the presence of a protein factor in this complex, which regulated the calspectin-F-actin interaction in a Ca2+- and calmodulin-dependent manner. Erythrocyte protein 4.1, but not synapsin I, mimics the function of this brain factor using a reconstitution system including purified calspectin, calmodulin and F-actin. In the brain complex, the Mr 120,000 and the Mr 80,000/77,000 polypeptides were detected to crossreact with anti-protein 4.1 antibody.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D001923:Brain Chemistry; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009479:Neuropeptides; D011485:Protein Binding; D016704:Synapsins; D014783:Viscosity
D000199:Actins; D001798:Blood Proteins; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D009479:Neuropeptides; D016704:Synapsins; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D002118:Calcium