title: DNase-I-dependent dissociation of erythrocyte cytoskeletons.
abstract: The human erythrocyte contains a complex of peripheral membrane proteins which forms an extensive network or cytoskeleton on the cytoplasmic membrane surface. When I treat erythrocyte cytoskeletons with deoxyribonuclease I (DNase I), the cytoskeletons dissociate and erythrocyte actin is solubilized. The dissociation of the cytoskeletons by DNase I parallels the disruption of actin filaments in vitro by DNase I and is blocked by the addition of action to the DNase I. Large protein complexes remain after DNase I disrupts the cytoskeletons, but these complexes are no longer visible in the light microscope nor sedimentable and are selectively depleted with respect to actin. From these studies, I suggest that DNase I binds to and solubilizes actin, which serves as a structural link between protein complexes in the erythrocyte cytoskeleton.
mesh_terms: D000199:Actins / Q000302:isolation & purification; D003851:Deoxyribonucleases / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D011489:Protein Denaturation; D012995:Solubility; D013347:Subcellular Fractions
chemical_list: D000199:Actins; D008565:Membrane Proteins; D003851:Deoxyribonucleases