REVIEW

Cell Research (2006)16: 872-878
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Hemicentins: What have we learned from worms?

Bruce E Vogel, Joaquin M Muriel, Chun Dong, Xuehong Xu

¹Program in Cell Structure and Development, Medical Biotechnology Center, University of Maryland Biotechnology Institute, 725 W. Lombard St., Baltimore, MD 21201, USA

Correspondence: Bruce E Vogel Tel: +1-410-706-4516; Fax: +1-410-706-8184; E-mail: vogel@umbi.umd.edu

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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.

Cell Research (2006) 16:872-878. doi:10.1038/sj.cr.7310110; published online 10 October 2006

Keywords: hemicentins, extracellular matrix, fibulin, cell junction and adhesion, C. elegans