TIRAP, an Adaptor Protein for TLR2/4, Transduces a Signal from RAGE Phosphorylated upon Ligand Binding
Author Information
Author(s): Sakaguchi Masakiyo, Murata Hitoshi, Yamamoto Ken-ichi, Ono Tomoyuki, Sakaguchi Yoshihiko, Motoyama Akira, Hibino Toshihiko, Kataoka Ken, Huh Nam-ho
Primary Institution: Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Hypothesis
How does the cytoplasmic domain of RAGE interact with TIRAP and MyD88 to regulate inflammation and immune response?
Conclusion
The study demonstrates that TIRAP and MyD88 are essential adaptor proteins for RAGE, facilitating signal transduction upon ligand binding.
Supporting Evidence
- The cytoplasmic domain of RAGE is phosphorylated at Ser391 by PKCĪ¶ upon ligand binding.
- TIRAP and MyD88 bind to phosphorylated RAGE and transduce signals to downstream molecules.
- Blocking TIRAP and MyD88 function abrogates intracellular signaling from ligand-activated RAGE.
Takeaway
When certain proteins bind to RAGE, they help send signals inside cells that can affect inflammation and immune responses.
Methodology
The study involved experiments with HEK293 cells to analyze the phosphorylation of RAGE and the binding of adaptor proteins.
Digital Object Identifier (DOI)
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