DNase I-dependent dissociation of erythrocyte cytoskeletons

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)266-270
Number of pages5
JournalJournal of Cell Biology
Volume81
Issue number1
DOIs
StatePublished - Jan 1 1979
Externally publishedYes

Fingerprint

Deoxyribonuclease I
Erythrocyte Membrane
Actins
Cytoskeleton
Actin Cytoskeleton
Membrane Proteins
Erythrocytes
Cell Membrane
Light
Proteins

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 journalArticle

@article{bee501949a01497092590ad322a90036,
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 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.",
author = "Michael Sheetz",
year = "1979",
month = "1",
day = "1",
doi = "10.1083/jcb.81.1.266",
language = "English (US)",
volume = "81",
pages = "266--270",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "1",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0018742929&partnerID=8YFLogxK

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

C2 - 479290

AN - SCOPUS:0018742929

VL - 81

SP - 266

EP - 270

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -