Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 43, Issue -, Pages 795-800Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20150071
Keywords
bone morphogenetic protein (BMP) signalling; chordin; tolloid cleavage
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Funding
- Biotechnology and Biological Sciences Research Council [BB/I019286/1]
- Wellcome Trust [106503/Z/14/Z]
- Deutsche Forschungsgemeinschaft [SFB829/Project B12]
- Wellcome Trust [106503/Z/14/Z] Funding Source: Wellcome Trust
- BBSRC [BB/I019286/1, BB/I012265/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I012265/1, BB/I019286/1] Funding Source: researchfish
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Chordin-mediated regulation of bone morphogenetic protein (BMP) family growth factors is essential in early embryogenesis and adult homoeostasis. Chordin binds to BMPs through cysteine-rich von Willebrand factor type C (vWC) homology domains and blocks them from interacting with their cell surface receptors. These domains also self-associate and enable chordin to target related proteins to fine-tune BMP regulation. The chordin-BMP inhibitory complex is strengthened by the secreted glycoprotein twisted gastrulation (Tsg); however, inhibition is relieved by cleavage of chordin at two specific sites by tolloid family metalloproteases. As Tsg enhances this cleavage process, it serves a dual role as both promoter and inhibitor of BMP signalling. Recent developments in chordin research suggest that rather than simply being by-products, the cleavage fragments of chordin continue to play a role in BMP regulation. In particular, chordin cleavage at the C-terminus potentiates its anti-BMP activity in a type-specific manner.
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