The Inositol Phosphatase SHIP-1 Inhibits NOD2-Induced NF-κB Activation by Disturbing the Interaction of XIAP with RIP2
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SHIP-1 is an inositol phosphatase predominantly expressed in hematopoietic cells. Over the ten past years, SHIP-1 has been described as an important regulator of immune functions. Here, we characterize a new inhibitory function for SHIP-1 in NOD2 signaling. NOD2 is a crucial cytoplasmic bacterial sensor that activates proinflammatory and antimicrobial responses upon bacterial invasion. We observed that SHIP-1 decreases NOD2-induced NF-κB activation in macrophages. This negative regulation relies on its interaction with XIAP. Indeed, we observed that XIAP is an essential mediator of the NOD2 signaling pathway that enables proper NF-κB activation in macrophages. Upon NOD2 activation, SHIP-1 C-terminal proline rich domain (PRD) interacts with XIAP, thereby disturbing the interaction between XIAP and RIP2 in order to decrease NF-κB signaling.
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SHIP1 inhibits NF-kB activation and subsequent induction of IL-6, IL-8 and TNF-α expression in human monocytes and mouse bone marrow-derived macrophages independent of its phosphatase activity.
“SHIP1 was found to inhibit NF-kB activation and the subsequent induction of IL-6, IL-8 and TNF-α expression in human monocytes and mouse bone marrow-derived macrophages independent of its phosphatase activity [130].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [130]
In Results, ‘SHIP-1 Downregulates NOD2-induced NF-κB Activation’ (page unavailable), SHIP-1 silencing increases MDP-induced NF-κB activity and IL-6, IL-8 and TNF-α mRNA in the human THP1 monocytic cell line. ‘SHIP-1 PRD Region is Necessary and Sufficient’ reports that inhibition does not require catalytic activity, but tests this in GNV cells. The copy does not show these SHIP-1 findings in mouse bone marrow-derived macrophages; its BMDM passage concerns XIAP deficiency instead. (LLM, conf=0.88)
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Pawar, P., Ratnakar, S., & Saxena, V. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177870
- Authors
- Condé, C., Rambout, X., Lebrun, M., Lecat, A., Di Valentin, E., Dequiedt, F., Piette, J., Gloire, G., & Legrand, S.
- Affiliations
- University of Liège (BE)
- Corresponding author
- Legrand, Sylvie
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-07-17
- Volume
- 7
- Issue
- 7
- Pages
- e41005
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3398883
- OpenAlex
- W2022192437
- Cited by
- 33
- References
- 55
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 3 · 2023: 3 · 2021: 1 · 2019: 3 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 5 · 2013: 4
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- ORBi (University of Liège) (submittedVersion, other-oa)
- Funders
- Fonds De La Recherche Scientifique - FNRS
- Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Keywords
- SHIP1, inositol phosphatase, NOD2 signaling, NF-κB activation, XIAP, RIP2, macrophages, proline-rich region, negative regulation of innate immunity, bacterial sensing, protein-protein interaction
- MeSH terms
- Inositol Polyphosphate 5-Phosphatases, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Epithelial Cells, Gene Expression Regulation, Humans, Immune System, Inflammation, Macrophages, Models, Biological, Monocytes, Phosphoric Monoester Hydrolases, Signal Transduction, Down-Regulation, NF-kappa B, Protein Structure, Tertiary, Cell Line, Tumor, X-Linked Inhibitor of Apoptosis Protein, Nod2 Signaling Adaptor Protein, Receptor-Interacting Protein Serine-Threonine Kinase 2
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