Interleukin-10 and Small Molecule SHIP1 Allosteric Regulators Trigger Anti-inflammatory Effects through SHIP1/STAT3 Complexes
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Abstract
The anti-inflammatory actions of interleukin-10 (IL10) are thought to be mediated primarily by the STAT3 transcription factor, but pro-inflammatory cytokines such as interleukin-6 (IL6) also act through STAT3. We now report that IL10, but not IL6 signaling, induces formation of a complex between STAT3 and the inositol polyphosphate-5-phosphatase SHIP1 in macrophages. Both SHIP1 and STAT3 translocate to the nucleus in macrophages. Remarkably, sesquiterpenes of the Pelorol family, which we previously described as allosteric activators of SHIP1 phosphatase activity, could induce SHIP1/STAT3 complex formation in cells and mimic the anti-inflammatory action of IL10 in a mouse model of colitis. Using crystallography and docking studies we identified a drug-binding pocket in SHIP1. Our studies reveal new mechanisms of action for both STAT3 and SHIP1 and provide a rationale for use of allosteric SHIP1-activating compounds, which mimic the beneficial anti-inflammatory actions of IL10. VIDEO ABSTRACT.
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In macrophages, IL-10 suppresses TNF-α secretion, which is promoted by both phosphatase-dependent and -independent activities of SHIP1.
“In macrophages, the anti-inflammatory cytokine IL-10 can suppress TNF-α secretion, which is promoted by both phosphatase-dependent and -independent activities of SHIP1 [131–133].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [133]
The Results section (“IL10 Requires Both SHIP1 and STAT3 to Inhibit Macrophage Production of TNFα”; page not provided) reports that IL-10 reduces TNFα in macrophages and that SHIP1 loss impairs this effect. The Discussion says SHIP1 with no detectable phosphatase activity is sufficient to mediate IL-10’s anti-inflammatory effect. It does not establish that phosphatase-dependent SHIP1 activity also promotes the IL-10-mediated suppression attributed to this source. (LLM, conf=0.86)
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Mopuru, R. (2023) · Indian Journal of Psychological Medicine · doi:10.1177/02537176231154270 · Cited by 1 · see citing works
The regulation of miR-155 strand selection by CELF2, FUBP1 and KSRP proteins
Yoon, J. S. J., Chamberlain, T. C., Lallous, N., & Mui, A. (2025) · Scientific Reports · doi:10.1038/s41598-025-15004-w · Cited by 1 · see citing works
Self-citationYoon, J. S. J., Baksh, A., Chamberlain, T. C., & Mui, A. (2021) · Preprints.org · doi:10.20944/preprints202111.0272.v1
Self-citationLiu, W., Jiang, H., Zhao, Q., Rui, H., Liu, B., & Dai, H. (2024) · Research Square · doi:10.21203/rs.3.rs-5653921/v1
Yoon, J. S. J., Baksh, A., Chamberlain, T. C., & Mui, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.05.641704
Self-citationDai, H., Liu, B., Rui, H., Yang, L., Jiang, H., Zhao, Q., & Liu, W. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1755723
- Authors
- Chamberlain, T. C., Cheung, S. T., Yoon, J. S. J., Ming-Lum, A., Gardill, B. R., Shakibakho, S., Dzananovic, E., Ban, F., Samiea, A., Jawanda, K., Priatel, J., Krystal, G., Ong, C. J., Cherkasov, A., Andersen, R. J., McKenna, S. A., Van Petegem, F., & Mui, A. L.-F.
- Affiliations
- University of British Columbia (CA)
- University of Manitoba (CA)
- Corresponding author
- Mui, Alice L-F.
- ORCID
- Venue
- iScience
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 23
- Issue
- 8
- Pages
- 101433
- ISSN
- 2589-0042 (ISSN-L)
- PMC
- PMC7452241
- OpenAlex
- W3046861920
- Cited by
- 32
- References
- 65
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 5 · 2022: 6 · 2021: 7
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- iScience (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Canadian Cancer Society (017289)
- National Research Council Canada
- Canadian Institutes of Health Research (MOP-84539)
- University of Saskatchewan
- Natural Sciences and Engineering Research Council of Canada
- Western Economic Diversification Canada
- Michael Smith Foundation for Health Research
- Canadian Cancer Society Research Institute
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Immunology and Microbiology › Immunology › Psoriasis: Treatment and Pathogenesis
- Keywords
- IL-10, SHIP1, STAT3, allosteric regulation, sesquiterpenes, macrophages, anti-inflammatory signaling, interleukin-6, colitis, drug-binding pocket, phosphatase activation, nuclear translocation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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