ArticleMolecular & cellular proteomics : MCP2016
Identification of RNA-binding Proteins in Macrophages by Interactome Capture.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 85 citations in OpenAlex.
- Key RNA-binding proteins in renal fibrosis: a comprehensive bioinformatics and machine learning framework for diagnostic and therapeutic insights.Renal failure · 2025Article
- Newborn apical resection preserves the proliferative capacity of cardiomyocytes located throughout the left ventricle.Stem cells (Dayton, Ohio) · 2025Article
- A Csde1-Strap complex regulates plasma cell differentiation by coupling mRNA translation and decay.Nature communications · 2025Article
- AMBRA1 controls the translation of immune-specific genes in T lymphocytes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lipopolysaccharide Regulates the Macrophage RNA-Binding Proteome.Journal of proteome research · 2024Article
- Refining the pool of RNA-binding domains advances the classification and prediction of RNA-binding proteins.Nucleic acids research · 2024Article
- Interrogation of RNA-protein interaction dynamics in bacterial growth.Molecular systems biology · 2024Article
- Regulation of inflammatory diseases via the control of mRNA decay.Inflammation and regeneration · 2024Review
- RNA Metabolism Governs Immune Function and Response.Advances in experimental medicine and biology · 2024Review
- Plant phase extraction: A method for enhanced discovery of the RNA-binding proteome and its dynamics in plants.The Plant cell · 2023Article
- HydRA: Deep-learning models for predicting RNA-binding capacity from protein interaction association context and protein sequence.Molecular cell · 2023Article
- Characterising the RNA-binding protein atlas of the mammalian brain uncovers RBM5 misregulation in mouse models of Huntington's disease.Nature communications · 2023Article
- Pyruvate Kinase M (PKM) binds ribosomes in a poly-ADP ribosylation dependent manner to induce translational stalling.Nucleic acids research · 2023Article
- The RNA-binding protein landscapes differ between mammalian organs and cultured cells.Nature communications · 2023Article
- Role of Heterogeneous Nuclear Ribonucleoproteins in the Cancer-Immune Landscape.International journal of molecular sciences · 2023Review
- Melanoma RBPome identification reveals PDIA6 as an unconventional RNA-binding protein involved in metastasis.Nucleic acids research · 2022Article
- Article
- RNA-binding proteins and their role in kidney disease.Nature reviews. Nephrology · 2022Review
- Computational tools to study RNA-protein complexes.Frontiers in molecular biosciences · 2022Review
- Opportunities and Challenges in Global Quantification of RNA-Protein InteractionFrontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
Pathogen components, such as lipopolysaccharides of Gram-negative bacteria that activate Toll-like receptor 4, induce mitogen activated protein kinases and NFκB through different downstream pathways to stimulate pro- and anti-inflammatory cytokine expression. Importantly, post-transcriptional control of the expression of Toll-like receptor 4 downstream signaling molecules contributes to the tight regulation of inflammatory cytokine synthesis in macrophages. Emerging evidence highlights the role of RNA-binding proteins (RBPs) in the post-transcriptional control of the innate immune response. To systematically identify macrophage RBPs and their response to LPS stimulation, we employed RNA interactome capture in LPS-induced and untreated murine RAW 264.7 macrophages. This combines RBP-crosslinking to RNA, cell lysis, oligo(dT) capture of polyadenylated RNAs and mass spectrometry analysis of associated proteins. Our data revealed 402 proteins of the macrophage RNA interactome including 91 previously not annotated as RBPs. A comparison with published RNA interactomes classified 32 RBPs uniquely identified in RAW 264.7 macrophages. Of these, 19 proteins are linked to biochemical activities not directly related to RNA. From this group, we validated the HSP90 cochaperone P23 that was demonstrated to exhibit cytosolic prostaglandin E2 synthase 3 (PTGES3) activity, and the hematopoietic cell-specific LYN substrate 1 (HCLS1 or HS1), a hematopoietic cell-specific adapter molecule, as novel macrophage RBPs. Our study expands the mammalian RBP repertoire, and identifies macrophage RBPs that respond to LPS. These RBPs are prime candidates for the post-transcriptional regulation and execution of LPS-induced signaling pathways and the innate immune response. Macrophage RBP data have been deposited to ProteomeXchange with identifier PXD002890.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.