ArticleeLife2015
Synthetic enzyme-substrate tethering obviates the Tolloid-ECM interaction during Drosophila BMP gradient formation.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Shrew is an essential, recently evolved, Drosophila specific gene required for formation of the embryonic BMP activity gradient.Developmental biology · 2026Article
- Molecular mechanism of BMP signal control by Twisted gastrulation.Nature communications · 2024Article
- Review
- Modelling the structure of Short Gastrulation and generation of a toolkit for studying its function in Drosophila.Biology open · 2022Article
- BMP antagonists in tissue development and disease.Matrix biology plus · 2021Review
- BMP Signaling: Lighting up the Way for Embryonic Dorsoventral Patterning.Frontiers in cell and developmental biology · 2021Review
- TGF-β Family Signaling in Early Vertebrate Development.Cold Spring Harbor perspectives in biology · 2018Review
- TGF-β Family Signaling inCold Spring Harbor perspectives in biology · 2017Review
- Control of signaling molecule range during developmental patterning.Cellular and molecular life sciences : CMLS · 2017Review
- Agonists and Antagonists of TGF-β Family Ligands.Cold Spring Harbor perspectives in biology · 2016Review
- Mammalian tolloid proteinases: role in growth factor signalling.FEBS letters · 2016Review
- Diversity between mammalian tolloid proteinases: Oligomerisation and non-catalytic domains influence activity and specificity.Scientific reports · 2016Article
- The role of chordin fragments generated by partial tolloid cleavage in regulating BMP activity.Biochemical Society transactions · 2015Review
- Article
- Peak BMP Responses in the Drosophila Embryo Are Dependent on the Activation of Integrin Signaling.Cell reports · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Members of the Tolloid family of metalloproteinases liberate BMPs from inhibitory complexes to regulate BMP gradient formation during embryonic dorsal-ventral axis patterning. Here, we determine mechanistically how Tolloid activity is regulated by its non-catalytic CUB domains in the Drosophila embryo. We show that Tolloid, via its N-terminal CUB domains, interacts with Collagen IV, which enhances Tolloid activity towards its substrate Sog, and facilitates Tsg-dependent stimulation of cleavage. In contrast, the two most C-terminal Tld CUB domains mediate Sog interaction to facilitate its processing as, based on our structural data, Tolloid curvature positions bound Sog in proximity to the protease domain. Having ascribed functions to the Tolloid non-catalytic domains, we recapitulate embryonic BMP gradient formation in their absence, by artificially tethering the Tld protease domain to Sog. Our studies highlight how the bipartite function of Tolloid CUB domains, in substrate and ECM interactions, fine-tune protease activity to a particular developmental context.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.