Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 20, Issue 1, Pages 78-89Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E08-05-0535
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- Deutsche Forschungsgemeinschaft [SFB 549]
- U.S. Public Health Service [DE016289]
- NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH [R01DE016289] Funding Source: NIH RePORTER
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Cell adhesion molecules such as cadherins alternate their expression throughout cranial neural crest (CNC) development, yet our understanding of the role of these molecules during CNC migration remains incomplete. The mesenchymal cadherin-11 is expressed in the CNC during migration yet prevents migration when overexpressed in the embryo, suggesting that a defined level of cadherin-11-mediated cell adhesion is required for migration. Here we show that members of the meltrin subfamily of ADAM metalloproteases cleave the extracellular domain of cadherin-11 during CNC migration. We show that a fragment corresponding to the putative shed form of cadherin-11 retains biological activity by promoting CNC migration in vivo, in a non-cell-autonomous manner. Additionally, cleavage of cadherin-11 does not affect binding to beta-catenin and downstream signaling events. We propose that ADAM cleavage of cadherin-11 promotes migration by modifying its ability to support cell-cell adhesion while maintaining the membrane-bound pool of beta-catenin associated with the cadherin-11 cytoplasmic domain.
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