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XB-ART-43059
Dev Cell 2011 Feb 15;202:256-63. doi: 10.1016/j.devcel.2010.12.009.
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Translocation of the cytoplasmic domain of ADAM13 to the nucleus is essential for Calpain8-a expression and cranial neural crest cell migration.



Abstract
ADAMs are transmembrane metalloproteases that control cell behavior by cleaving both cell adhesion and signaling molecules. The cytoplasmic domain of ADAMs can regulate the proteolytic activity by controlling the subcellular localization and/or the activation of the protease domain. Here, we show that the cytoplasmic domain of ADAM13 is cleaved and translocates into the nucleus. Preventing this translocation renders the protein incapable of promoting cranial neural crest (CNC) cell migration in vivo, without affecting its proteolytic activity. In addition, the cytoplasmic domain of ADAM13 regulates the expression of multiple genes in CNC, including the protease Calpain8-a. Restoring the expression of Calpain8-a is sufficient to rescue CNC migration in the absence of the ADAM13 cytoplasmic domain. This study shows that the cytoplasmic domain of ADAM metalloproteases can perform essential functions in the nucleus of cells and may contribute substantially to the overall function of the protein.

PubMed ID: 21316592
PMC ID: PMC3074609
Article link: Dev Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: adam13 adam19 adam9 camk1 capn8.1 dap dusp18 fst mmp13 nubp1 nudc parp1 pcdh8.2 pou3f1 rad1 tbx2 vamp8 wnt3 xmc
Antibodies: Adam13 Ab7
Morpholinos: adam13 MO3 adam19 MO2

GEO Series: GSE21517: NCBI

Article Images: [+] show captions
References [+] :
Abe, NMDA-receptor activation induces calpain-mediated beta-catenin cleavages for triggering gene expression. 2007, Pubmed