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Development ePress online publication date 5 Jan 2005
doi: 10.1242/dev.01599


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Research article

XPACE4 is a localized pro-protein convertase required for mesoderm induction and the cleavage of specific TGF{beta} proteins in Xenopus development


Bilge Birsoy, Linnea Berg, P. Huw Williams, James C. Smith, Christopher C. Wylie, Jan L. Christian, and Janet Heasman*
* Author for correspondence (e-mail: heabq9{at}chmcc.org)

XPACE4 is a member of the subtilisin/kexin family of pro-protein convertases. It cleaves many pro-proteins to release their active proteins, including members of the TGF{beta} family of signaling molecules. Studies in mouse suggest it may have important roles in regulating embryonic tissue specification. Here, we examine the role of XPACE4 in Xenopus development and make three novel observations: first, XPACE4 is stored as maternal mRNA localized to the mitochondrial cloud and vegetal hemisphere of the oocyte; second, it is required for the endogenous mesoderm inducing activity of vegetal cells before gastrulation; and third, it has substrate-specific activity, cleaving Xnr1, Xnr2, Xnr3 and Vg1, but not Xnr5, Derrière or ActivinB pro-proteins. We conclude that maternal XPACE4 plays an important role in embryonic patterning by regulating the production of a subset of active mature TGF{beta} proteins in specific sites.


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