ArticleDevelopmental biology2012
Two functional domains in C. elegans glypican LON-2 can independently inhibit BMP-like signaling.
Article in Developmental biology, 2012. 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, 17 citations in OpenAlex.
- SMOC-1 interacts with both BMP and glypican to regulate BMP signaling in C. elegans.PLoS biology · 2023Article
- Article
- Deletion of the RGD motif in LON-2/glypican is associated with morphological abnormalities.microPublication biology · 2021Article
- AP2M1 Supports TGF-β Signals to Promote Collagen Expression by Inhibiting Caveolin Expression.International journal of molecular sciences · 2021Article
- Functional Requirements for Heparan Sulfate Biosynthesis in Morphogenesis and Nervous System Development in C. elegans.PLoS genetics · 2017Article
- Agonists and Antagonists of TGF-β Family Ligands.Cold Spring Harbor perspectives in biology · 2016Review
- Article
- Glypican Is a Modulator of Netrin-Mediated Axon Guidance.PLoS biology · 2015Article
- Insights into the key roles of proteoglycans in breast cancer biology and translational medicine.Biochimica et biophysica acta · 2015Review
- Regulation of extracellular matrix organization by BMP signaling in Caenorhabditis elegans.PloS one · 2014Article
- Repulsive guidance molecules (RGMs) and neogenin in bone morphogenetic protein (BMP) signaling.Molecular reproduction and development · 2013Review
- Regulation of TGFβ superfamily signaling by two separable domains of glypican LON-2 in C. elegans.Worm · 2013Article
- High-resolution analysis and functional mapping of cleavage sites and substrate proteins of furin in the human proteome.PloS one · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Glypicans are multifunctional proteoglycans with regulatory roles in several intercellular signaling pathways. Here, we examine the functional requirements for glypican regulation of bone morphogenetic protein (BMP)-mediated body length in C. elegans. We provide evidence that two parts of C. elegans glypican LON-2 can independently inhibit BMP signaling in vivo: the N-terminal furin protease product and the C-terminal region containing heparan sulfate attachment sequences. While the C-terminal protease product is dispensable for LON-2 minimal core protein activity, it does affect the localization of LON-2. Cleavage of LON-2 into two parts at the conserved furin protease site is not required for LON-2 to inhibit BMP-like signaling. The glycosyl-phosphatidylinositol (GPI) membrane anchor is also not absolutely required for LON-2 activity. Finally, we show that an RGD protein-protein interaction motif in the LON-2 N-terminal domain is necessary for LON-2 core protein activity, suggesting that LON-2 inhibits BMP signaling by acting as a scaffold for BMP and an RGD-binding protein.
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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.