ArticleProceedings of the National Academy of Sciences of the United States of America2005
Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor.
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 102 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
102 citing papers in PubMed, 222 citations in OpenAlex.
- Spatial microenvironments tune immune response dynamics in the Drosophila larval fat body.PLoS genetics · 2026Article
- Chemical modulation of IMD signaling in the cat flea (Current research in insect science · 2026Article
- Commensal bacterial glycosylation at the interface of host-bacteria interactions.Gut microbes · 2025Review
- Layers of immunity: Deconstructing theeLife · 2025Article
- Spatial microenvironments tune immune response dynamics in thebioRxiv : the preprint server for biology · 2025Article
- Stem cell-specific NF-κB is required for stem cell survival and epithelial regeneration upon intestinal damage.Biology open · 2025Article
- Loss of the NF-κB negative regulator Pirk inBrain communications · 2025Article
- Pattern recognition receptors in Crustacea: immunological roles under environmental stress.Frontiers in immunology · 2024Review
- Integrated analysis of miRNA profiles and gut bacterial changes inEcology and evolution · 2023Article
- Steroid hormone regulation of innate immunity in Drosophila melanogaster.PLoS genetics · 2023Review
- Regulating metabolism to shape immune function: Lessons from Drosophila.Seminars in cell & developmental biology · 2023Review
- Potential biomarker proteins for aspiration pneumonia detected by shotgun proteomics using buccal mucosa samples: a cross-sectional case-control study.Clinical proteomics · 2023Article
- Drosophila caspases as guardians of host-microbe interactions.Cell death and differentiation · 2023Review
- Drosophila hemocytes recognize lymph gland tumors of mxc mutants and activate the innate immune pathway in a reactive oxygen species-dependent manner.Biology open · 2022Article
- The circular RNA Edis regulates neurodevelopment and innate immunity.PLoS genetics · 2022Article
- M1-linked ubiquitination facilitates NF-κB activation and survival during sterile inflammation.The FEBS journal · 2022Article
- Review
- Beneficial commensal bacteria promote Drosophila growth by downregulating the expression of peptidoglycan recognition proteins.iScience · 2022Article
- Antimicrobial peptide expression in the cockroach gut during enterobacterial infection is specific and influenced by type III secretion.Biology open · 2022Article
- A peptidoglycan-recognition protein orchestrates the first steps of symbiont recruitment in the squid-vibrio symbiosis.Symbiosis (Philadelphia, Pa.) · 2022Article
42 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Drosophila peptidoglycan recognition protein LC (PGRP-LC), a transmembrane protein required for the response to bacterial infection, acts at the top of a cytoplasmic signaling cascade that requires the death-domain protein Imd and an IkappaB kinase to activate Relish, an NF-kappaB family member. It is not clear how binding of peptidoglycan to the extracellular domain of PGRP-LC activates intracellular signaling because its cytoplasmic domain has no homology to characterized proteins. Here, we demonstrate that PGRP-LC binds Imd and that its cytoplasmic domain is critical for its activity, suggesting that PGRP-LC acts as a signal-transducing receptor. The PGRP-LC cytoplasmic domain is also essential for the formation of dimers, and results suggest that dimerization may be required for receptor activation. The PGRP-LC cytoplasmic domain can mediate formation of heterodimers between different PGRP-LC isoforms, thereby potentially expanding the diversity of ligands that can be recognized by the receptor.
Indexed as
Identifiers
What OpenQuestion holds
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.