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XB-ART-15804
Cell October 31, 1997; 91 (3): 407-16.

Cleavage of Chordin by Xolloid metalloprotease suggests a role for proteolytic processing in the regulation of Spemann organizer activity.

Piccolo S , Agius E , Lu B , Goodman S , Dale L , De Robertis EM .


Abstract
The Xolloid secreted metalloprotease, a tolloid-related protein, was found to cleave Chordin and Chordin/BMP-4 complexes at two specific sites in biochemical experiments Xolloid mRNA blocks secondary axes caused by chordin, but not by noggin, follistatin, or dominant-negative BMP receptor, mRNA injection. Xolloid-treated Chordin protein was unable to antagonize BMP activity. Furthermore, Xolloid digestion released biologically active BMPs from Chordin/BMP inactive complexes. Injection of dominant-negative Xolloid mRNA indicated that the in vivo function of Xolloid is to limit the extent of Spemann''s organizer field. We propose that Xolloid regulates organizer function by a novel proteolytic mechanism involving a double inhibition pathway required to pattern the dorsoventral axis: [formula in text].

PubMed ID: 9363949
PMC ID: PMC3070600
Article link: Cell
Grant support: [+]
Genes referenced: bmp1 bmp4 bmp7.1 chrd.1 fst krt12.4 myod1 ncam1 nog shh snai2 sox2 tbxt tll2 wnt8a


Article Images: [+] show captions
References [+] :
Biehs, The Drosophila short gastrulation gene prevents Dpp from autoactivating and suppressing neurogenesis in the neuroectoderm. 1996, Pubmed, Xenbase


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