Abstract
Abstract TLR3 (Toll-like receptor 3) belongs to the family of receptors involved in innate immune response. Present in endosomal compartment in cells, TLR3 recognizes the dsRNA (double-stranded RNA), viral nucleic acid or intermediate during viral replication and initiates signal transduction leading to inflammatory response. However, the first steps of signaling cascade occurring in cells immediately after TLR3 stimulation are still not well understood and require careful attention. In this paper we demonstrate that after poly(I:C) (dsRNA mimetic) stimulation of murine microglial cells (C8D1A cell line) tyrosine kinase Syk interacts with Hrs (hepatocyte growth factor regulated tyrosine kinase substrate), one of the ESCRT-0 (endosomal sorting complex required for transportation-0) components. This protein complex was recently implicated in trafficking of other endosomal TLRs, TLR7 and TLR9, and plays a possible role in the TLR3 signaling. Phosphorylation of Hrs, which is a very likely result of Hrs-Syk interaction, also takes place after poly(I:C) stimulation, strongly suggesting that an association between activated TLR3 and ESCRT-0 exists. Therefore, Hrs may influence TLR3 signaling pathways, but this requires further investigation.
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