Golgi spectrin: identification of an erythroid beta-spectrin homolog associated with the Golgi complex.
J Cell Biol
; 127(3): 707-23, 1994 Nov.
Article
en En
| MEDLINE
| ID: mdl-7962054
ABSTRACT
Spectrin is a major component of a membrane-associated cytoskeleton involved in the maintenance of membrane structural integrity and the generation of functionally distinct membrane protein domains. Here, we show that a homolog of erythrocyte beta-spectrin (beta I sigma*) co-localizes with markers of the Golgi complex in a variety of cell types, and that microinjected beta-spectrin codistributes with elements of the Golgi complex. Significantly, we show a dynamic relationship between beta-spectrin and the structural and functional organization of the Golgi complex. Disruption of both Golgi structure and function, either in mitotic cells or following addition of brefeldin A, is accompanied by loss of beta-spectrin from Golgi membranes and dispersal in the cytoplasm. In contrast, perturbation of Golgi structure without a loss of function, by the addition of nocodazole, results in retention of beta-spectrin with the dispersed Golgi elements. These results indicate that the association of beta-spectrin with Golgi membranes is coupled to Golgi organization and function.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Espectrina
/
Aparato de Golgi
/
Hígado
Tipo de estudio:
Diagnostic_studies
/
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
J Cell Biol
Año:
1994
Tipo del documento:
Article