| Publications from the Jorgensen Laboratory |  |  |
| Authors | Hammarlund M, Davis WS, Jorgensen EM. |
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| Title | Mutations in beta-spectrin disrupt axon outgrowth and sarcomere structure |
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| Year | 2000-05-15 |
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| Journal | J Cell Biol |
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| Volume | 149(4) |
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| Pages | 931-942 |
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| PDF | [PDF-996 KB] |
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beta-Spectrin is a major component of the membrane skeleton, a structure found at the plasma membrane of most animal cells. beta-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 beta-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, beta-spectrin is not essential for general membrane integrity or for cell polarity. However, beta-spectrin is required for a subset of processes at cell membranes. In neurons, the loss of beta-spectrin leads to abnormal axon outgrowth. In muscles, a loss of beta-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 beta-spectrin function in anchoring proteins at cell membranes.
Todd Harris, PhD ( harris@cshl.org )
updated: Fri Nov 12 09:26:38 2004