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Structure and regulation of cytoplasmic adapter proteins involved in innate immune signaling
Author(s) -
Monie Tom P.,
Moncrieffe Martin C.,
Gay Nicholas J.
Publication year - 2009
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.2008.00735.x
Subject(s) - innate immune system , biology , signal transduction , signal transducing adaptor protein , microbiology and biotechnology , pattern recognition receptor , receptor , immune system , immune receptor , adapter (computing) , toll like receptor , immunology , genetics , engineering , electrical engineering
Summary: Initiation of the innate immune response requires agonist recognition by a pathogen recognition receptor. Following ligand binding, conformational rearrangement of the receptor creates a molecular scaffold from which signal transduction is propagated via complex cellular signaling pathways. This in turn leads to the induction of a pro‐inflammatory immune response. A critical component of these signaling pathways is the homotypic interaction of receptor and adapter proteins via specific protein interaction domains. Within the innate immune signaling cascade, homotypic interactions between members of the death domain family and the Toll/interleukin‐1 receptor domain are particularly important. Here we discuss the current understanding of the molecular basis of these homotypic receptor:adapter interactions and their role in innate immune signal transduction.