作者: Bilge Birsoy , Linnea Berg , P Huw Williams , James C Smith , Christopher C Wylie
DOI: 10.1242/DEV.01599
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摘要: XPACE4 is a member of the subtilisin/kexin family pro-protein convertases. It cleaves many pro-proteins to release their active proteins, including members TGFβ signaling molecules. Studies in mouse suggest it may have important roles in regulating embryonic tissue specification. Here, we examine role Xenopus development and make three novel observations: first, is stored as maternal mRNA localized mitochondrial cloud vegetal hemisphere oocyte; second, required for endogenous mesoderm inducing activity vegetal cells before gastrulation; third, has substrate-specific activity, cleaving Xnr1, Xnr2, Xnr3 Vg1, but not Xnr5, Derriere or ActivinB pro-proteins. We conclude that XPACE4 plays an patterning by production of subset mature proteins specific sites.