Ka. Beck et al., GOLGI SPECTRIN - IDENTIFICATION OF AN ERYTHROID BETA-SPECTRIN HOMOLOGASSOCIATED WITH THE GOLGI-COMPLEX, The Journal of cell biology, 127(3), 1994, pp. 707-723
Spectrin is a major component of a membrane-associated cytoskeleton in
volved in the maintenance of membrane structural integrity and the gen
eration of functionally distinct membrane protein domains. Here, we sh
ow that a homolog of erythrocyte beta-spectrin (beta I Sigma) co-loca
lizes with markers of the Golgi complex in a variety of cell types, an
d that microinjected beta-spectrin codistributes with elements of the
Golgi complex. Significantly, we show a dynamic relationship between b
eta-spectrin and the structural and functional organization of the Gol
gi 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 cytop
lasm. In contrast, perturbation of Golgi structure without a loss of f
unction, by the addition of nocodazole, results in retention of beta-s
pectrin with the dispersed Golgi elements. These results indicate that
the association of beta-spectrin with Golgi membranes is coupled to G
olgi organization and function.