Essential roles of S100A10 in Toll-like receptor signaling and immunity to infection

Lou, Yunwei; Han, Meijuan; Liu, Huandi; Niu, Yuna; Liang, Yinming; Guo, Jun; Zhang, Wen; Wang, Hui

doi:10.1038/s41423-019-0278-1

Cited by 49 publications

(31 citation statements)

References 39 publications

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“…Luciferase reporter gene assays were performed as described previously [41]. Briefly, HEK293 cells were transfected with an IFN-β/ISRE luciferase reporter plasmid and a Renilla luciferase plasmid as an internal control plus the indicated plasmids.…”

Section: Luciferase Reporter Gene Assaymentioning

confidence: 99%

RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation

et al. 2020

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Mediator of IRF3 activation (MITA, also named as STING/ERIS/MPYS/TMEM173), is essential to DNA virus-or cytosolic DNA-triggered innate immune responses. In this study, we demonstrated the negative regulatory role of RING-finger protein (RNF) 90 in innate immune responses targeting MITA. RNF90 promoted K48-linked ubiquitination of MITA and its proteasome-dependent degradation. Overexpression of RNF90 inhibited HSV-1-or cytosolic DNA-induced immune responses whereas RNF90 knockdown had the opposite effects. Moreover, RNF90-deficient bone marrow-derived dendritic cells (BMDCs), bone marrow-derived macrophages (BMMs) and mouse embryonic fibroblasts (MEFs) exhibited increased DNA virus-or cytosolic DNA-triggered signaling and RNF90 deficiency protected mice from DNA virus infection. Taken together, our findings suggested a novel function of RNF90 in innate immunity. OPEN ACCESS Citation: Yang B, Liu Y, Cui Y, Song D, Zhang G, Ma S, et al. (2020) RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation. PLoS Pathog 16(3): e1008387.

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Section: Luciferase Reporter Gene Assaymentioning

confidence: 99%

RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation

et al. 2020

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“…Bone marrow-derived macrophages (BMDMs) were generated as described (17,29). The purity of BMDMs was more than 95% as determined by CD11b + and F4/80 + flow cytometry staining.…”

Section: Cell Culture and Transfectionmentioning

confidence: 99%

The SCFβ-TrCP E3 Ubiquitin Ligase Regulates Immune Receptor Signaling by Targeting the Negative Regulatory Protein TIPE2

Lou

Han

Song

et al. 2020

The Journal of Immunology

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TNFAIP8-like 2 (TIPE2) is a negative regulator of immune receptor signaling that maintains immune homeostasis. Dysregulated TIPE2 expression has been observed in several types of human immunological disorders. However, how TIPE2 expression is regulated remains to be determined. We report in this study that the SCF b-TrCP E3 ubiquitin ligase regulates TIPE2 protein abundance by targeting it for ubiquitination and subsequent degradation via the 26S proteasome. Silencing of either cullin-1 or b-TrCP1 resulted in increased levels of TIPE2 in immune cells. TAK1 phosphorylated the Ser 3 in the noncanonical degron motif of TIPE2 to trigger its interaction with b-TrCP for subsequent ubiquitination and degradation. Importantly, the amount of TIPE2 protein in immune cells determined the strength of TLR 4-induced signaling and downstream gene expression. Thus, our study has uncovered a mechanism by which SCF b-TrCP E3 ubiquitin ligase regulates TLR responses.

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“…Anti-inflammatory related Cfl1, Gng12, Manf, and Ptpn6 proteins show high expression in the S3 state and then decrease again. Notably, S100a10, Rps28, Irg1, and Ptgs2 proteins increase the amount of abundance from S4 to S3, which is the most active period of macrophages, showing that cells at that time have a proinflammatory function 31, 40, 41 . Through trajectory analysis, we found that Arglu1, Nip7, Nudcd2, and Mtmr2 proteins, whose functions are not yet known for the activation of macrophages, elevate in S4 and then gradually decrease with time.…”

Section: Resultsmentioning

confidence: 99%

Robust, sensitive, and quantitative single-cell proteomics based on ion mobility filtering

Woo

Williams

et al. 2021

Preprint

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Unbiased single-cell proteomics (scProteomics) promises to advance our understanding of the cellular composition of complex biological systems. However, a major challenge for current methods is their ability to identify and provide accurate quantitative information for low abundance proteins. Herein, we describe an ion mobility-enhanced mass spectrometry acquisition method, TIFF (Transferring Identification based on FAIMS Filtering), designed to improve the sensitivity and accuracy of label-free scProteomics. The TIFF method enabled unbiased proteome analysis to a depth of >1,700 proteins in single HeLa cells with >1,100 proteins consistently quantified, a significant improvement in overall performance. We applied the TIFF method to obtain temporal proteome profiles of >150 single murine macrophage cells during a lipopolysaccharide stimulation experiment and uncovered unanticipated temporal response trajectories. Further, we demonstrated, to our knowledge, the first application of scProteomics to classify cell populations of a human organ (the lung) without prior antibody labeling.

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Essential roles of S100A10 in Toll-like receptor signaling and immunity to infection

Cited by 49 publications

References 39 publications

RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation

RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation

The SCFβ-TrCP E3 Ubiquitin Ligase Regulates Immune Receptor Signaling by Targeting the Negative Regulatory Protein TIPE2

Robust, sensitive, and quantitative single-cell proteomics based on ion mobility filtering

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