DNase I-dependent dissociation of erythrocyte cytoskeletons

Research output: Contribution to journalArticle

22 Scopus citations

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

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'DNase I-dependent dissociation of erythrocyte cytoskeletons'. Together they form a unique fingerprint.

  • Cite this