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Published 23 July 2001. doi:10.1083/jcb.200007075
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© The Rockefeller University Press, 0021-9525/2001/7/403 $5.00
The Journal of Cell Biology, Volume 154, Number 2, July 23, 2001 403-414

Article

MUP-4 is a novel transmembrane protein with functions in epithelial cell adhesion in Caenorhabditis elegans



Leexan Hong1, Tricia Elbl1, James Ward1, Clara Franzini-Armstrong1, Krystyna K. Rybicka1, Beth K. Gatewood2, David L. Baillie3 and Elizabeth A. Bucher1

1 Department of Cell and Developmental Biology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104
2 Department of Biology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104
3 Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada

Address correspondence to Elizabeth A. Bucher, Department of Cell and Developmental Biology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6058. Tel.: (215) 898-2136. Fax: (215) 898-9871. E-mail: bucher{at}mail.med.upenn.edu

Tissue functions and mechanical coupling of cells must be integrated throughout development. A striking example of this coupling is the interactions of body wall muscle and hypodermal cells in Caenorhabditis elegans. These tissues are intimately associated in development and their interactions generate structures that provide a continuous mechanical link to transmit muscle forces across the hypodermis to the cuticle. Previously, we established that mup-4 is essential in embryonic epithelial (hypodermal) morphogenesis and maintenance of muscle position. Here, we report that mup-4 encodes a novel transmembrane protein that is required for attachments between the apical epithelial surface and the cuticular matrix. Its extracellular domain includes epidermal growth factor-like repeats, a von Willebrand factor A domain, and two sea urchin enterokinase modules. Its intracellular domain is homologous to filaggrin, an intermediate filament (IF)-associated protein that regulates IF compaction and that has not previously been reported as part of a junctional complex. MUP-4 colocalizes with epithelial hemidesmosomes overlying body wall muscles, beginning at the time of embryonic cuticle maturation, as well as with other sites of mechanical coupling. These findings support that MUP-4 is a junctional protein that functions in IF tethering, cell–matrix adherence, and mechanical coupling of tissues.

Key Words: filaggrin; intermediate filaments; hemidesmosomes; cell adhesion; muscle force transmission


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