ArticleMolecular & cellular proteomics : MCP2019
Quantification of Dynamic Protein Interactions and Phosphorylation in LPS Signaling Pathway by SWATH-MS.
Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Quantitative Modeling of TLR Signaling Reveals Missing Negative Feedback Guiding Identification of TANK-IKKε Checkpoint.bioRxiv : the preprint server for biology · 2026Article
- Phosphoproteomic profiling of lipopolysaccharide stimulated toll-like receptor pathways in macrophages.Scientific data · 2025Article
- Bioactive Polysaccharides Prevent Lipopolysaccharide-Induced Intestinal Inflammation via Immunomodulation, Antioxidant Activity, and Microbiota Regulation.Foods (Basel, Switzerland) · 2025Article
- MiR-146a engineered extracellular vesicles derived from mesenchymal stromal cells more potently attenuate ischaemia-reperfusion injury in lung transplantation.Clinical and translational medicine · 2025Article
- Data-Driven Modeling Identifies TIRAP-Independent MyD88 Activation Complex and Myddosome Assembly Strategy in LPS/TLR4 Signaling.International journal of molecular sciences · 2020Article
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Authors and funding
18 authors at 1 institution in 1 country.
Funding
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Abstract
Lipopolysaccharide (LPS)-induced macrophage activation is a prototype of innate immune response. Although key effector proteins in LPS signaling pathway have been revealed, the map of dynamic protein interactions and phosphorylation as well as the stoichiometry of protein complexes are lacking. Here we present a dynamic map of protein interactions and phosphorylation in MyD88, TRAF6 and NEMO complexes obtained by SWATH-MS. The comprehensive MS measurement leads to quantification of up to about 3,000 proteins across about 21-40 IP samples. We detected and quantified almost all known interactors of MyD88, TRAF6 and NEMO. By analyzing these quantitative data, we uncovered differential recruitment of IRAK family proteins to LPS-induced signaling complexes and determined the stoichiometry of the Myddosome complex. In addition, quantitative phosphoproteomics analysis identified a number of unreported high-confidence phosphosites on the key proteins in LPS signaling pathway. Collectively, data of dynamic protein interactions and phosphorylation presented by this study could be a resource for further study of the LPS signaling pathway.
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