ArticleProceedings of the National Academy of Sciences of the United States of America2005
Bursicon, the insect cuticle-hardening hormone, is a heterodimeric cystine knot protein that activates G protein-coupled receptor LGR2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 265 citations in OpenAlex.
- A Tale of Two States: Similarities and Differences in Neuropeptide Signaling in Larval and Adult Drosophila.The Journal of comparative neurology · 2026Review
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- Two neuropeptides that promote blood feeding ineLife · 2026Article
- Gene Expression ofInternational journal of molecular sciences · 2026Article
- ETH and Burs-α are necessary for the normal molting inFrontiers in insect science · 2026Article
- Article
- Inducing bursicon expression using 20-hydroxyecdysone (20E) increased immune response in Macrobrachium rosenbergii against Aeromonas hydrophila.Biology open · 2025Article
- Neuropeptide Bursicon and its receptor-mediated the transition from summer-form to winter-form ofeLife · 2024Article
- Cephalic ganglia transcriptomics of the American cockroach Periplaneta americana (Blattodea: Blattidae).Journal of insect science (Online) · 2024Article
- LGR signaling mediates muscle-adipose tissue crosstalk and protects against diet-induced insulin resistance.Nature communications · 2024Article
- NeuronalCells · 2023Article
- LGR4: A New Receptor Member in Endocrine and Metabolic Diseases.Endocrine reviews · 2023Review
- Crystal structure of LGR ligand α2/β5 fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Identification and characterization of ecdysis-related neuropeptides in the lone star tickFrontiers in endocrinology · 2023Article
- Article
- Modeling exercise using optogenetically contractible Drosophila larvae.BMC genomics · 2022Article
- A natural genetic variation screen identifies insulin signaling, neuronal communication, and innate immunity as modifiers of hyperglycemia in the absence of Sirt1.G3 (Bethesda, Md.) · 2022Article
- Review: The evolution of peptidergic signaling in Cnidaria and Placozoa, including a comparison with Bilateria.Frontiers in endocrinology · 2022Review
- Fluorescent Microscopy-Based Detection of Chitin in IntactFrontiers in physiology · 2022Article
- LGR4, a G Protein-Coupled Receptor With a Systemic Role: From Development to Metabolic Regulation.Frontiers in endocrinology · 2022Review
38 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
All arthropods periodically molt to replace their exoskeleton (cuticle). Immediately after shedding the old cuticle, the neurohormone bursicon causes the hardening and darkening of the new cuticle. Here we show that bursicon, to our knowledge the first heterodimeric cystine knot hormone found in insects, consists of two proteins encoded by the genes burs and pburs (partner of burs). The pburs/burs heterodimer from Drosophila melanogaster binds with high affinity and specificity to activate the G protein-coupled receptor DLGR2, leading to the stimulation of cAMP signaling in vitro and tanning in neck-ligated blowflies. Native bursicon from Periplaneta americana is also a heterodimer. In D. melanogaster the levels of pburs, burs, and DLGR2 transcripts are increased before ecdysis, consistent with their role in postecdysial cuticle changes. Immunohistochemical analyses in diverse insect species revealed the colocalization of pburs- and burs-immunoreactivity in some of the neurosecretory neurons that also express crustacean cardioactive peptide. Forty-three years after its initial description, the elucidation of the molecular identity of bursicon and the verification of its receptor allow for studies of bursicon actions in regulating cuticle tanning, wing expansion, and as yet unknown functions. Because bursicon subunit genes are homologous to the vertebrate bone morphogenetic protein antagonists, our findings also facilitate investigation on the function of these proteins during vertebrate development.
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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.