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Vol. 8, Issue 10, 1933-1942, October 1997
Department of Pharmacological and Physiological Sciences and the
Committees on Cell Physiology and Developmental Biology, University of
Chicago, Chicago, Illinois 60637
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 
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 (
H),
which is constitutively associated with the plasma membrane in S2
cells. Another membrane marker, the Na,K-ATPase, codistributes with
ankyrin and 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, spectrin, and the Na,K-ATPase colocalize at the lateral
domain of salivary gland cells. In contrast, 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.
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