Authors: | Choe, K. M.; Lee, H.; Anderson, K. V. |
Article Title: | Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor |
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 lmd and an IκB kinase to activate Relish, an NF-κB 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 lmd 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. |
Keywords: | signal transduction; unclassified drug; nonhuman; protein domain; animal cell; animals; protein; protein binding; drosophila; immunoglobulin enhancer binding protein; bacteria (microorganisms); animalia; molecular recognition; carrier proteins; membrane protein; cytoplasm; innate immunity; dimerization; receptor; sequence homology; heterodimer; bacterial infection; drosophila proteins; isoprotein; i kappa b kinase; nf-κb; dimer; lmd; immunity, natural; peptidoglycan; relish; death domain protein; imd protein; immune receptor; peptidoglycan recognition protein lc; relish protein; signal transducing receptor |
Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
Volume: | 102 |
Issue: | 4 |
ISSN: | 0027-8424 |
Publisher: | National Academy of Sciences |
Date Published: | 2005-01-25 |
Start Page: | 1122 |
End Page: | 1126 |
Language: | English |
DOI: | 10.1073/pnas.0404952102 |
PUBMED: | 15657141 |
PROVIDER: | scopus |
PMCID: | PMC545828 |
DOI/URL: | |
Notes: | --- - "Cited By (since 1996): 66" - "Export Date: 24 October 2012" - "CODEN: PNASA" - "Source: Scopus" |