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XB-ART-8150
Genes Dev 2001 Nov 01;1521:2797-802. doi: 10.1101/gad.940001.
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The activity and signaling range of mature BMP-4 is regulated by sequential cleavage at two sites within the prodomain of the precursor.

Cui Y, Hackenmiller R, Berg L, Jean F, Nakayama T, Thomas G, Christian JL.


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Proteolytic maturation of proBMP-4 is required to generate an active signaling molecule. We show that proBMP-4 is cleaved by furin in a sequential manner. Cleavage at a consensus furin site adjacent to the mature ligand domain allows for subsequent cleavage at an upstream nonconsensus furin site within the prodomain. BMP-4 synthesized from precursor in which the upstream site is noncleavable is less active, signals at a shorter range, and accumulates at lower levels than does BMP-4 cleaved from native precursor. Conversely, BMP-4 cleaved from precursor in which both sites are rapidly cleaved is more active and signals over a greater range. Differential use of the upstream cleavage site could provide for tissue-specific regulation of BMP-4 activity and signaling range.

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Species referenced: Xenopus
Genes referenced: bmp4 furin

References [+] :
Anderson, Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. 1997, Pubmed