ArticleInternational journal of molecular sciences2020
Data-Driven Modeling Identifies TIRAP-Independent MyD88 Activation Complex and Myddosome Assembly Strategy in LPS/TLR4 Signaling.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 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
- Roles of TIR domain-containing adaptor protein in tumor: Inflammation and immune regulation via toll-like receptor signaling.The Journal of international medical research · 2026Review
- ADSC-Conditioned Medium Mitigates LPS-Induced Acute Lung Injury by Inhibiting Alveolar Macrophage Pyroptosis.Current issues in molecular biology · 2026Article
- SeFilter-DIA: Squeeze-and-Excitation Network for Filtering High-Confidence Peptides of Data-Independent Acquisition Proteomics.Interdisciplinary sciences, computational life sciences · 2024Article
- Oxomollugin, an oxidized substance in mollugin, inhibited LPS-induced NF-κB activation via the suppressive effects on essential activation factors of TLR4 signaling.Journal of natural medicines · 2024Article
- scGIR: deciphering cellular heterogeneity via gene ranking in single-cell weighted gene correlation networks.Briefings in bioinformatics · 2024Article
- Bacterial lipopolysaccharide-induced endothelial activation and dysfunction: a new predictive and therapeutic paradigm for sepsis.European journal of medical research · 2023Review
- Comparative characterization of microRNA-71 of Echinococcus granulosus exosomes.Parasite (Paris, France) · 2023Article
- Dear-DIAResearch (Washington, D.C.) · 2023Article
- The role and mechanisms of gram-negative bacterial outer membrane vesicles in inflammatory diseases.Frontiers in immunology · 2023Review
- Network modeling-based identification of the switching targets between pyroptosis and secondary pyroptosis.Chaos, solitons, and fractals · 2022Article
- Nanocurcumin alleviates inflammation and oxidative stress in LPS-induced mastitis via activation of Nrf2 and suppressing TLR4-mediated NF-κB and HMGB1 signaling pathways in rats.Environmental science and pollution research international · 2022Article
- Quantifying the optimal strategy of population control of quorum sensing network in Escherichia coli.NPJ systems biology and applications · 2021Article
- Aureusidin derivative CNQX inhibits chronic colitis inflammation and mucosal barrier damage by targeting myeloid differentiation 2 protein.Journal of cellular and molecular medicine · 2021Article
- TIRAP in the Mechanism of Inflammation.Frontiers in immunology · 2021Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TLR4 complexes are essential for the initiation of the LPS-induced innate immune response. The Myddosome, which mainly contains TLR4, TIRAP, MyD88, IRAK1/4 and TRAF6 proteins, is regarded as a major complex of TLR4. Although the Myddosome has been well studied, a quantitative description of the Myddosome assembly dynamics is still lacking. Furthermore, whether some unknown TLR4 complexes exist remains unclear. In this study, we constructed a SWATH-MS data-based mathematical model that describes the component assembly dynamics of TLR4 complexes. In addition to Myddosome, we suggest that a TIRAP-independent MyD88 activation complex is formed upon LPS stimulation, in which TRAF6 is not included. Furthermore, quantitative analysis reveals that the distribution of components in TIRAP-dependent and -independent MyD88 activation complexes are LPS stimulation-dependent. The two complexes compete for recruiting IRAK1/4 proteins. MyD88 forms higher-order assembly in the Myddosome and we show that the strategy to form higher-order assembly is also LPS stimulation-dependent. MyD88 forms a long chain upon weak stimulation, but forms a short chain upon strong stimulation. Higher-order assembly of MyD88 is directly determined by the level of TIRAP in the Myddosome, providing a formation mechanism for efficient signaling transduction. Taken together, our study provides an enhanced understanding of component assembly dynamics and strategies in TLR4 complexes.
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