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© The Rockefeller University Press, 0021-9525/2000//647 $5.00
The Journal of Cell Biology, Volume 149, Number 3, , 2000 647-656

Original Article

Drosophila β Spectrin Functions Independently of {alpha} Spectrin to Polarize the Na,k Atpase in Epithelial Cells



Ronald R. Dubreuila, Ping Wanga, Steve Dahlb, John Leeb, and Lawrence S.B. Goldsteinb

a Department of Neurobiology, Pharmacology, and Physiology, University of Chicago, Chicago, Illinois 60637
b Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Pharmacology, School of Medicine, University of California San Diego, La Jolla, California 92093-0683
Department of Neurobiology, Pharmacology, and Physiology, The University of Chicago, 947 E. 58th Street, MC 0926, Chicago, IL 60637.(773) 702-3774(773) 702-9154

ron{at}drugs.bsd.uchicago.edu

Spectrin has been proposed to function as a sorting machine that concentrates interacting proteins such as the Na,K ATPase within specialized plasma membrane domains of polarized cells. However, little direct evidence to support this model has been obtained. Here we used a genetic approach to directly test the requirement for the β subunit of the {alpha}β spectrin molecule in morphogenesis and function of epithelial cells in Drosophila. β Spectrin mutations were lethal during late embryonic/early larval development and they produced subtle defects in midgut morphology and stomach acid secretion. The polarized distributions of {alpha}βH spectrin and ankyrin were not significantly altered in β spectrin mutants, indicating that the two isoforms of Drosophila spectrin assemble independently of one another, and that ankyrin is upstream of {alpha}β spectrin in the spectrin assembly pathway. In contrast, β spectrin mutations had a striking effect on the basolateral accumulation of the Na,K ATPase. The results establish a role for β spectrin in determining the subcellular distribution of the Na,K ATPase and, unexpectedly, this role is independent of {alpha} spectrin.

Key Words: cell polarity • cytoskeleton • Drosophila melanogaster • plasma membrane • ankyrins

© 2000 The Rockefeller University Press

S. Dahl's current address is Division of Nephrology, Johns Hopkins School of Medicine, Baltimore, MD 21205.

Abbreviation used in this paper: GFP, green fluorescent protein.


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