C. elegansankyrin repeat protein VAB-19 is a component of epidermal attachment structures and is essential for epidermal morphogenesis

• DOI: 10.1242/dev.00791
• Publication Date: 2003-10-14T00:17:43Z
• Authors: Mei Ding; Alexandr Goncharov; Yishi Jin; Andrew D. Chisholm
• Keywords: 0301 basic medicine; Recombinant Fusion Proteins; Molecular Sequence Data; Spectrin; Actins; Ankyrin Repeat; Cytoskeletal Proteins; 03 medical and health sciences; Morphogenesis; Animals; Humans; Amino Acid Sequence; Epidermis; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Sequence Alignment; Cytoskeleton; Body Patterning

Elongation of the epidermis of the nematode Caenorhabditis elegansinvolves 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.