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First published online 8 October 2003
doi: 10.1242/dev.00791
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1 Sinsheimer Laboratories, Department of Molecular, Cellular, and Developmental
Biology, University of California, Santa Cruz, CA 95064, USA
2 Howard Hughes Medical Institute, Department of Molecular, Cellular, and
Developmental Biology, University of California, Santa Cruz, CA 95064,
USA
* Author for correspondence (e-mail: chisholm{at}biology.ucsc.edu)
Accepted 11 August 2003
Elongation of the epidermis of the nematode Caenorhabditis elegans involves both actomyosin-mediated changes in lateral epidermal cell shape and body muscle attachment to dorsal and ventral epidermal cells via intermediate-filament/hemidesmosome structures. vab-19 mutants are defective in epidermal elongation and muscle attachment to the epidermis. VAB-19 is a member of a conserved family of ankyrin repeat-containing proteins that includes the human tumor suppressor Kank. In epidermal cells, VAB-19::GFP localizes with components of epidermal attachment structures. In vab-19 mutants, epidermal attachment structures form normally but do not remain localized to muscle-adjacent regions of the epidermis. VAB-19 localization requires function of the transmembrane attachment structure component Myotactin. vab-19 mutants also display aberrant actin organization in the epidermis. Loss of function in the spectrin SMA-1 partly bypasses the requirement for VAB-19 in elongation, suggesting that VAB-19 and SMA-1/spectrin might play antagonistic roles in regulation of the actin cytoskeleton.
Key words: C. elegans, Epidermis, Morphogenesis, Ankyrin repeat, Spectrin
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