ArticleMatrix biology : journal of the International Society for Matrix Biology2016
Structural characterization of twisted gastrulation provides insights into opposing functions on the BMP signalling pathway.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Whole-genome resequencing with multidimensional annotation revealed pathogenic networks in sirenomelia.Italian journal of pediatrics · 2026Article
- Molecular mechanism of BMP signal control by Twisted gastrulation.Nature communications · 2024Article
- Reconstitution of morphogen shuttling circuits.Science advances · 2023Article
- Multifaceted Functions of TWSG1: From Embryogenesis to Cancer Development.International journal of molecular sciences · 2022Review
- BMP antagonists in tissue development and disease.Matrix biology plus · 2021Review
- Tumor Promoting Effect of BMP Signaling in Endometrial Cancer.International journal of molecular sciences · 2021Article
- I22: SAXS/WAXS beamline at Diamond Light Source - an overview of 10 years operation.Journal of synchrotron radiation · 2021Article
- BMP Signaling: Lighting up the Way for Embryonic Dorsoventral Patterning.Frontiers in cell and developmental biology · 2021Review
- Review
- Bone Morphogenetic Protein-2 in Development and Bone Homeostasis.Journal of developmental biology · 2020Review
- Internal cleavage and synergy with twisted gastrulation enhance BMP inhibition by BMPER.Matrix biology : journal of the International Society for Matrix Biology · 2019Article
- TGF-β Family Signaling in Early Vertebrate Development.Cold Spring Harbor perspectives in biology · 2018Review
- Mammalian tolloid proteinases: role in growth factor signalling.FEBS letters · 2016Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Twisted gastrulation (Tsg) and chordin are secreted glycoproteins that function together as BMP (bone morphogenetic protein) antagonists to regulate BMP growth factor signalling. Chordin binds to BMPs, preventing them from interacting with their receptors and Tsg is known to strengthen this inhibitory complex. Tsg also acts as a BMP agonist by promoting cleavage of chordin by tolloid-family proteinases. Here we explore the structural mechanism through which Tsg exerts this dual activity. We have characterized the nanoscale structure of human Tsg using in-solution biomolecular analysis and show that Tsg is a globular monomer with a flattened cross shape. Tsg has a high proportion of N-linked glycans, in relation to its molecular weight, which supports a role in solubilising BMPs. Tsg binds with high affinity to the C-terminal region of chordin and was also able to inhibit BMP-7 signalling directly but did not have an effect on BMP-4 signalling. Although both Tsg and mammalian tolloid are involved in chordin cleavage, no interaction could be detected between them using surface plasmon resonance. Together these data suggest that Tsg functions as a BMP-agonist by inducing conformational change in chordin making it more susceptible to tolloid cleavage and as a BMP-antagonist either independently or via a chordin-mediated mechanism. Following single cleavage of chordin by tolloids, Tsg continues to strengthen the inhibitory complex, supporting a role for partially cleaved chordin in BMP regulation.
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Registered trials
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