Segregation of two spectrin isoforms: polarized membrane-binding sites direct polarized membrane skeleton assembly

• Published in: Molecular biology of the cell 1997-10, Vol.8 (10), p.1933-1942
• Main Authors: Dubreuil, R R, Maddux, P B, Grushko, T A, MacVicar, G R
• Format: Article
• Language: English
• Subjects: Animals; Ankyrins - analysis; Ankyrins - metabolism; Binding Sites; Cell Adhesion Molecules, Neuronal - analysis; Cell Adhesion Molecules, Neuronal - genetics; Cell Adhesion Molecules, Neuronal - metabolism; Cell Line; Cell Membrane - chemistry; Cytoskeleton - chemistry; Cytoskeleton - metabolism; Drosophila; Drosophila Proteins; Epithelial Cells - chemistry; Humans; Isomerism; Oocytes - chemistry; Salivary Glands - chemistry; Salivary Glands - cytology; Sodium-Potassium-Exchanging ATPase - analysis; Sodium-Potassium-Exchanging ATPase - metabolism; Spectrin - analysis; Spectrin - chemistry; Spectrin - metabolism; Tissue Distribution
• ISSN: 1059-1524; 1939-4586
• DOI: 10.1091/mbc.8.10.1933

Spectrin isoforms are often segregated within specialized plasma membrane subdomains where they are thought to contribute to the development of cell surface polarity. It was previously shown that ankyrin and beta spectrin are recruited to sites of cell-cell contact in Drosophila S2 cells expressing the homophilic adhesion molecule neuroglian. Here, we show that neuroglian has no apparent effect on a second spectrin isoform (alpha beta H), which is constitutively associated with the plasma membrane in S2 cells. Another membrane marker, the Na,K-ATPase, codistributes with ankyrin and alpha beta spectrin at sites of neuroglian-mediated contact. The distributions of these markers in epithelial cells in vivo are consistent with the order of events observed in S2 cells. Neuroglian, ankyrin, alpha beta spectrin, and the Na,K-ATPase colocalize at the lateral domain of salivary gland cells. In contrast, alpha beta H spectrin is sorted to the apical domain of salivary gland and somatic follicle cells. Thus, the two spectrin isoforms respond independently to positional cues at the cell surface: in one case an apically sorted receptor and in the other case a locally activated cell-cell adhesion molecule. The results support a model in which the membrane skeleton behaves as a transducer of positional information within cells.