ArticleDevelopment (Cambridge, England)2012
Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing.
Article in Development (Cambridge, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Shrew is an essential, recently evolved, Drosophila specific gene required for formation of the embryonic BMP activity gradient.Developmental biology · 2026Article
- Evidence for vitellogenin DNA-binding in honey bees.Protein science : a publication of the Protein Society · 2025Article
- Lipidome Unsaturation Affects the Morphology and Proteome of theJournal of proteome research · 2024Article
- Review
- Comparative Analyses of Reproductive Caste Types Reveal Vitellogenin Genes Involved in Queen Fertility inInternational journal of molecular sciences · 2023Article
- Review
- Drosophila ML-DmD17-c3 cells respond robustly to Dpp and exhibit complex transcriptional feedback on BMP signaling components.BMC developmental biology · 2019Article
- TGF-β Family Signaling inCold Spring Harbor perspectives in biology · 2017Review
- Scribbled Optimizes BMP Signaling through Its Receptor Internalization to the Rab5 Endosome and Promote Robust Epithelial Morphogenesis.PLoS genetics · 2016Article
- Article
- Extracellular distribution of diffusible growth factors controlled by heparan sulfate proteoglycans during mammalian embryogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Insights into the molecular mechanisms underlying diversified wing venation among insects.Proceedings. Biological sciences · 2014Article
- Strategies for exploring TGF-β signaling in Drosophila.Methods (San Diego, Calif.) · 2014Review
- Transcriptional profiling of reproductive development, lipid storage and molting throughout the last juvenile stage of the marine copepod Calanus finmarchicus.Frontiers in zoology · 2014Article
- Vitellogenin family gene expression does not increase Drosophila lifespan or fecundity.F1000Research · 2014Article
- Analysis of Drosophila glucuronyl C5-epimerase: implications for developmental roles of heparan sulfate sulfation compensation and 2-O-sulfated glucuronic acid.The Journal of biological chemistry · 2013Article
- The Drosophila wings apart gene anchors a novel, evolutionarily conserved pathway of neuromuscular development.Genetics · 2013Article
- Fine-tuned shuttles for bone morphogenetic proteins.Current opinion in genetics & development · 2013Review
- New insights into extracellular and post-translational regulation of TGF-β family signalling pathways.Journal of biochemistry · 2013Review
- A feed-forward loop coupling extracellular BMP transport and morphogenesis in Drosophila wing.PLoS genetics · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The sensitivity of the posterior crossvein in the pupal wing of Drosophila to reductions in the levels and range of BMP signaling has been used to isolate and characterize novel regulators of this pathway. We show here that crossveinless d (cv-d) mutations, which disrupt BMP signaling during the development of the posterior crossvein, mutate a lipoprotein that is similar to the vitellogenins that comprise the major constituents of yolk in animal embryos. Cv-d is made in the liver-like fat body and other tissues, and can diffuse into the pupal wing via the hemolymph. Cv-d binds to the BMPs Dpp and Gbb through its Vg domain, and to heparan sulfate proteoglycans, which are well-known for their role in BMP movement and accumulation in the wing. Cv-d acts over a long range in vivo, and does not have BMP co-receptor-like activity in vitro. We suggest that, instead, it affects the range of BMP movement in the pupal wing, probably as part of a lipid-BMP-lipoprotein complex, similar to the role proposed for the apolipophorin lipid transport proteins in Hedgehog and Wnt movement.
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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.