AI Article Synopsis
- RAGE activation creates a chronic inflammation signal linked to various diseases, highlighting the need to understand its cellular signaling processes.
- The study discovered that the ligand binding and cytoplasmic areas of RAGE are separate, requiring receptor oligomerization for activation.
- Using advanced techniques, researchers identified a specific region in the oligomeric form of RAGE that contributes to its structure, leading to a proposed model for how RAGE dimers and larger structures form.
Article Abstract
Activation of the receptor for advanced glycation end products (RAGE) leads to a chronic proinflammatory signal, affecting patients with a variety of diseases. Potentially beneficial modification of RAGE activity requires understanding the signal transduction mechanism at the molecular level. The ligand binding domain is structurally uncoupled from the cytoplasmic domain, suggesting receptor oligomerization is a requirement for receptor activation. In this study, we used hydrogen-deuterium exchange and mass spectrometry to map structural differences between the monomeric and oligomeric forms of RAGE. Our results indicated the presence of a region shielded from exchange in the oligomeric form of RAGE and led to the identification of a new oligomerization interface localized at the linker region between domains C1 and C2. Based on this finding, a model of a RAGE dimer and higher oligomeric state was constructed.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788119 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0076353 | PLOS |
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