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 actin 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.
Original language | English (US) |
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Pages (from-to) | 266-270 |
Number of pages | 5 |
Journal | Journal of Cell Biology |
Volume | 81 |
Issue number | 1 |
DOIs | |
State | Published - 1979 |
Externally published | Yes |
ASJC Scopus subject areas
- Cell Biology