The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase.
Open accessAbstract
A 145-kDa tyrosine-phosphorylated protein that becomes associated with Shc in response to multiple cytokines has been purified from the murine hemopoietic cell line B6SUtA1. Amino acid sequence data were used to clone the cDNA encoding this protein from a B6SUtA1 library. The predicted amino acid sequence encodes a unique protein containing an N-terminal src homology 2 domain, two consensus sequences that are targets for phosphotyrosine binding domains, a proline-rich region, and two motifs highly conserved among inositol polyphosphate 5-phosphatases. Cell lysates immunoprecipitated with antiserum to this protein exhibited both phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate polyphosphate 5-phosphatase activity. This novel signal transduction intermediate may serve to modulate both Ras and inositol signaling pathways. Based on its properties, we suggest the 145-kDa protein be called SHIP for SH2-containing inositol phosphatase.
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SHIP1 was originally observed in hematopoietic cells after cytokines and growth factors induced tyrosine phosphorylation of this 145-kDa protein.
“SHIP1 was originally observed in hematopoietic cells after a variety of cytokines and growth factors induced the tyrosine phosphorylation of this 145-kDa protein [98–104].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [103]
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The IL-4 receptor: signaling mechanisms and biologic functions
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Structure, function, and biology of SHIP proteins
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Genetics ignite focus on microglial inflammation in Alzheimer’s disease
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INPP5D regulates inflammasome activation in human microglia
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Pan-SHIP1/2 inhibitors promote microglia effector functions essential for CNS homeostasis
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- Authors
- Damen, J. E., Liu, L., Rosten, P., Humphries, R. K., Jefferson, A. B., Majerus, P. W., & Krystal, G.
- Affiliations
- BC Cancer Agency (CA)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1996-02-20
- Volume
- 93
- Issue
- 4
- Pages
- 1689-1693
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC40003
- OpenAlex
- W2058924545
- Cited by
- 633
- References
- 2
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 7 · 2023: 12 · 2022: 5 · 2021: 2 · 2020: 4 · 2019: 8 · 2018: 11 · 2017: 11 · 2016: 14 · 2015: 14 · 2014: 9 · 2013: 21 · 2012: 22
- FWCI
- 22.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p50hl014147-25)
- Medical Research Council
- BC Cancer Agency
- National Heart, Lung, and Blood Institute (HL-16634, HL14147)
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Keywords
- ships, Shc, inositol tetrakisphosphate, phosphatidylinositol 3,4,5-trisphosphate, inositol polyphosphate 5-phosphatase, cytokine signaling, Ras signaling, signal transduction, SH2 domain, tyrosine phosphorylation, cDNA cloning
- MeSH terms
- Src Homology 2 Domain-Containing, Transforming Protein 1, Inositol Polyphosphate 5-Phosphatases, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Genes, Inositol Phosphates, Interleukin-3, Molecular Sequence Data, Phosphoric Monoester Hydrolases, Protein Binding, Proteins, Recombinant Fusion Proteins, Recombinant Proteins, Signal Transduction, Granulocyte-Macrophage Colony-Stimulating Factor, Consensus Sequence, DNA, Complementary, Phosphatidylinositol Phosphates, src Homology Domains, Phosphotyrosine, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing, Mice, Shc Signaling Adaptor Proteins
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