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

 Kwang-Min Choe  ;  Hyangkyu Lee  ;  Kathryn V. Anderson 
 Proceedings of the National Academy of Sciences of the United States of America, Vol.102(4) : 1122-1126, 2005 
Journal Title
 Proceedings of the National Academy of Sciences of the United States of America 
Issue Date
Animals ; Carrier Proteins/chemistry ; Carrier Proteins/physiology* ; Dimerization ; Drosophila/immunology* ; Drosophila Proteins/chemistry ; Drosophila Proteins/physiology ; Immunity, Innate* ; Signal Transduction*
Imd ; innate immunity ; NF-κB ; Relish
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 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 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.
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3. College of Nursing (간호대학) > Dept. of Nursing (간호학과) > 1. Journal Papers
Yonsei Authors
Lee, Hyang Kyu(이향규) ORCID logo https://orcid.org/0000-0002-0821-6020
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