The role of band 4.1 in the association of actin with erythrocyte membranes.
Biochim Biophys Acta
; 688(3): 691-701, 1982 Jun 28.
Article
en En
| MEDLINE
| ID: mdl-6889438
ABSTRACT
Spectrin stimulates the association of F-actin with erythrocyte inside-out vesicles. Although inside-out vesicles are nearly devoid of two of the three major cytoskeletal proteins, spectrin and actin, they retain nearly all of the cytoskeletal protein designated band 4.1. Inside-out vesicles which have been substantially depleted of band 4.1 by extraction in 1 M KCl, 0.4 M urea and then reconstituted with spectrin show a markedly diminished ability to bind actin by comparison with vesicles containing normal amounts of band 4.1. This diminution is not due to an impaired ability of the vesicles to bind spectrin. Addition of purified band 4.1 to vesicles either before or after they have been reconstituted with spectrin restores their actin binding capacity to near normal levels as does addition of a spectrin-band 4.1 complex prepared by sucrose gradient centrifugation. Band 4.1 bound to vesicles in the absence of added spectrin has no effect on actin binding. Our results suggest that a spectrin band 4.1 complex is responsible for binding actin to erythrocyte membranes.
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Banco de datos:
MEDLINE
Asunto principal:
Neuropéptidos
/
Proteínas Sanguíneas
/
Actinas
/
Espectrina
/
Proteínas del Citoesqueleto
/
Membrana Eritrocítica
/
Eritrocitos
/
Proteínas de la Membrana
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1982
Tipo del documento:
Article