Abstract
Hemicentins are conserved extracellular matrix proteins discovered in Caenorhabditis elegans, with orthologs in all vertebrate species including human and mouse. Hemicentins share a single, highly conserved amino-terminal von Willebrand A domain, followed by a long (>40) stretch of immunoglobulin repeats, multiple tandem epidermal growth factors and a fibulin-like carboxy-terminal module. C. elegans has a single hemicentin gene that has pleiotropic functions in transient cell contacts that are required for cell migration and basement membrane invasion and in stable contacts at hemidesmosome-mediated cell junctions and elastic fiber-like structures. Here, we summarize what is known about the function of hemicentin in C. elegans and discuss implications for hemicentin function in other species. © 2006 IBCB, SIBS, CAS All rights reserved.
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Vogel, B. E., Muriel, J. M., Dong, C., & Xu, X. (2006, November). Hemicentins: What have we learned from worms? Cell Research. https://doi.org/10.1038/sj.cr.7310100
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