The Journal of Cell Biology, Vol 81, 266-270, Copyright © 1979 by The Rockefeller University Press
DNase-I-dependent dissociation of erythrocyte cytoskeletons
MP Sheetz
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.
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