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© The Rockefeller University Press, 0021-9525/2000/5/931/ $5.00
The Journal of Cell Biology, Volume 149, Number 4, May 15, 2000 931-942


Original Article

Mutations in ß-Spectrin Disrupt Axon Outgrowth and Sarcomere Structure

Marc Hammarlunda, Warren S. Davisa, and Erik M. Jorgensena
a Department of Biology, University of Utah, Salt Lake City, Utah 84112-0840

Correspondence to: Erik M. Jorgensen, Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112-0840. Tel:(801) 585-3517 Fax:(801) 581-4668 E-mail:jorgensen{at}biology.utah.edu.

ß-Spectrin is a major component of the membrane skeleton, a structure found at the plasma membrane of most animal cells. ß-Spectrin and the membrane skeleton have been proposed to stabilize cell membranes, generate cell polarity, or localize specific membrane proteins. We demonstrate that the Caenorhabditis elegans homologue of ß-spectrin is encoded by the unc-70 gene. unc-70 null mutants develop slowly, and the adults are paralyzed and dumpy. However, the membrane integrity is not impaired in unc-70 animals, nor is cell polarity affected. Thus, ß-spectrin is not essential for general membrane integrity or for cell polarity. However, ß-spectrin is required for a subset of processes at cell membranes. In neurons, the loss of ß-spectrin leads to abnormal axon outgrowth. In muscles, a loss of ß-spectrin leads to disorganization of the myofilament lattice, discontinuities in the dense bodies, and a reduction or loss of the sarcoplasmic reticulum. These defects are consistent with ß-spectrin function in anchoring proteins at cell membranes.

Key Words: unc-70, Caenorhabditis elegans, cytoskeleton, neurons, muscles


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