Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor

Kwang-Min Choe, Hyangkyu Lee, Kathryn V. Anderson

Research output: Contribution to journalArticle

126 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1122-1126
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number4
DOIs
Publication statusPublished - 2005 Jan 25

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Proteins
Peptidoglycan
Dimerization
peptidoglycan recognition protein
Bacterial Infections
Protein Isoforms
Phosphotransferases
Ligands
Death Domain

All Science Journal Classification (ASJC) codes

  • Genetics
  • General

Cite this

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