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.
Article| April 01 1979
DNase-I-dependent dissociation of erythrocyte cytoskeletons.
M P Sheetz
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1979) 81 (1): 266–270.
M P Sheetz; DNase-I-dependent dissociation of erythrocyte cytoskeletons.. J Cell Biol 1 April 1979; 81 (1): 266–270. doi: https://doi.org/10.1083/jcb.81.1.266
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