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 β-spectrin (βIΣ*) co-localizes with markers of the Golgi complex in a variety of cell types, and that microinjected β- spectrin codistributes with elements of the Golgi complex. Significantly, we show a dynamic relationship between β-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 β-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 β-spectrin with the dispersed Golgi elements. These results indicate that the association of β-spectrin with Golgi membranes is coupled to Golgi organization and function.
ASJC Scopus subject areas
- Cell Biology