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) |
|---|---|
| Pages (from-to) | 266-270 |
| Number of pages | 5 |
| Journal | Journal of Cell Biology |
| Volume | 81 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1979 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
Cite this
DNase I-dependent dissociation of erythrocyte cytoskeletons. / Sheetz, Michael.
In: Journal of Cell Biology, Vol. 81, No. 1, 01.01.1979, p. 266-270.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - DNase I-dependent dissociation of erythrocyte cytoskeletons
AU - Sheetz, Michael
PY - 1979/1/1
Y1 - 1979/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0018742929&partnerID=8YFLogxK
U2 - 10.1083/jcb.81.1.266
DO - 10.1083/jcb.81.1.266
M3 - Article
VL - 81
SP - 266
EP - 270
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 1
ER -