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First published online 5 January 2005
doi: 10.1242/dev.01599

Development 132, 591-602 (2005)
Published by The Company of Biologists 2005
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XPACE4 is a localized pro-protein convertase required for mesoderm induction and the cleavage of specific TGFß proteins in Xenopus development

Bilge Birsoy1, Linnea Berg2, P. Huw Williams3, James C. Smith4, Christopher C. Wylie1, Jan L. Christian2 and Janet Heasman1,*

1 Division of Developmental Biology, Cincinnati Children's Hospital Research Foundation, 3333 Burnet Avenue, Cincinnati, OH 45229, USA
2 Department of Cell and Developmental Biology, Oregon Health and Science University, Portland, OR 97201, USA
3 Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK
4 Wellcome Trust/Cancer Research Gurdon UK Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, UK

* Author for correspondence (e-mail: heabq9{at}chmcc.org)

Accepted 29 November 2004

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 TGFß 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 TGFß proteins in specific sites.

Key words: PACE4, TGFß, Mesoderm induction, Vg1


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XPACE4: regulating TGFß signalling by cleavage

Development 2005 132: e304. [Full Text]  



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