Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIP

Lamkin, Thomas D.; Walk, Scott F.; Liu, Ling; Damen, Jacqueline E.; Krystal, Gerald; Ravichandran, Kodimangalam S.

doi:10.1074/jbc.272.16.10396

Cited by 118Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingT-cell and B-cell Immunology

Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIP

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Lamkin, Thomas D., Walk, Scott F., Liu, Ling, Damen, Jacqueline E., Krystal, Gerald, Ravichandran, Kodimangalam S.·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.16.10396

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Abstract

The adapter protein Shc has been implicated in mitogenic signaling via growth factor receptors, cytokine receptors, and antigen receptors on lymphocytes. Besides the well characterized interaction of Shc with molecules involved in Ras activation, Shc also associates with a 145-kDa tyrosine-phosphorylated protein upon triggering via antigen receptors and many cytokine receptors. This 145-kDa protein has been recently identified as an SH2 domain containing 5'-inositol phosphatase (SHIP) and has been implicated in the regulation of growth and differentiation in hematopoietic cells. In this report, we have addressed the molecular details of the interaction between Shc and SHIP in vivo. During T cell receptor signaling, tyrosine phosphorylation of SHIP and its association with Shc occurred only upon activation. We demonstrate that the phosphotyrosine binding domain of Shc is necessary and sufficient for its association with tyrosine-phosphorylated SHIP. Through site-directed mutagenesis, we have identified two tyrosines on SHIP, Tyr-917, and Tyr-1020, as the principal contact sites for the Shc-phosphotyrosine binding domain. Our data also suggest a role for the tyrosine kinase Lck in phosphorylation of SHIP. We also show that the SH2 domain of SHIP is dispensable for the Shc-SHIP interaction in vivo. These data have implications for the localization of the Shc.SHIP complex and regulation of SHIP function during T cell receptor signaling.

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Phosphorylation at Tyr1022 within the NPxY motif allows SHIP1 to bind PTB domain-containing proteins.
“while phosphorylation at Tyr1022 (Tyr1020 in mice) within the NPxY motif allows SHIP1 to bind PTB domain-containing proteins [111, 112], as well as SHIP1’s own SH2 domain [113].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [111]
The Tyr-917/Tyr-1020 binding experiments and conclusion (Fig. 4; page not provided) show that phosphorylation of SHIP Tyr-1020 contributes to binding the PTB domain of Shc. The paper does not establish the human Tyr-1022 numbering or binding to PTB domain-containing proteins beyond Shc. (LLM, conf=0.86)
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Recruitment and Phosphorylation of SH2-Containing Inositol Phosphatase and Shc to the B-Cell Fcϒ Immunoreceptor Tyrosine-Based Inhibition Motif Peptide Motif
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PTP‐PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates
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Inhibitor and activator: dual functions for SHIP in immunity and cancer
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Regulation of immune cell signaling by SHIP1: A phosphatase, scaffold protein, and potential therapeutic target
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Evidence for a Requirement for Both Phospholipid and Phosphotyrosine Binding via the Shc Phosphotyrosine-Binding Domain In Vivo
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The role of SHIP in cytokine-induced signaling
Kalesnikoff, J., Sly, L. M., Hughes, M. R., Büchse, T., Rauh, M. J., Cao, L.-P., Lam, V., Mui, A., Huber, M. C., & Krystal, G. (2003) · Springer eBooks · doi:10.1007/s10254-003-0016-y · Cited by 101 · see citing works
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CDw150 Associates with Src-Homology 2-Containing Inositol Phosphatase and Modulates CD95-Mediated Apoptosis
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Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease
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The Src homology 2 domain–containing inositol 5-phosphatase negatively regulates Fcγ receptor–mediated phagocytosis through immunoreceptor tyrosine-based activation motif–bearing phagocytic receptors
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PTEN, but not SHIP and SHIP2, suppresses the PI3K/Akt pathway and induces growth inhibition and apoptosis of myeloma cells
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Tyrosine Phosphorylation and Relocation of SHIP Are Integrin-mediated in Thrombin-stimulated Human Blood Platelets
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An SH2 Domain-Containing 5′ Inositolphosphatase Inhibits Insulin-Induced GLUT4 Translocation and Growth Factor-Induced Actin Filament Rearrangement
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The SH2-Containing Inositol Polyphosphate 5-Phosphatase, Ship, Is Expressed During Hematopoiesis and Spermatogenesis
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Inositol Polyphosphate Phosphatases in Human Disease
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Negative signaling in B cells: SHIP Grbs Shc
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ERK Phosphorylates p66shcA on Ser36 and Subsequently Regulates p27kip1Expression via the Akt-FOXO3a Pathway: Implication of p27kip1in Cell Response to Oxidative Stress
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Integrin-mediated Ras–Extracellular Regulated Kinase (ERK) Signaling Regulates Interferon γ Production in Human Natural Killer Cells
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SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
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Downstream of Tyrosine Kinases-1 and Src Homology 2-Containing Inositol 5′-Phosphatase Are Required for Regulation of CD4+CD25+ T Cell Development
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Regulation of the immune response by SHIP
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Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion
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Failure to induce organ-specific autoimmunity by breaking of tolerance: importance of the microenvironment
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The role of SHIP in growth factor induced signalling
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Essential Role for the C-Terminal Noncatalytic Region of SHIP in FcγRIIB1-Mediated Inhibitory Signaling
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The Src Homology Domain 2-Containing Inositol Phosphatase SHIP Forms a Ternary Complex with Shc and Grb2 in Antigen Receptor-stimulated B Lymphocytes
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Src Homology 2 Domain-Containing Inositol Polyphosphate Phosphatase Regulates NF-κB-Mediated Gene Transcription by Phagocytic FcγRs in Human Myeloid Cells
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Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcgammaRIIb in B cells.
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SHIP1, an SH2 Domain Containing Polyinositol-5-phosphatase, Regulates Migration through Two Critical Tyrosine Residues and Forms a Novel Signaling Complex with DOK1 and CRKL
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Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5′-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I
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Activation/Inhibition of mast cells by supra-optimal antigen concentrations
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A Novel Spliced Form of SH2-Containing Inositol Phosphatase Is Expressed During Myeloid Development
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Differential signaling through p190 and p210 BCR-ABL fusion proteins revealed by interactome and phosphoproteome analysis
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Protein Interactions of Src Homology 2 (SH2) Domain-Containing Inositol Phosphatase (SHIP): Association with Shc Displaces SHIP from FcγRIIb in B Cells
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The SH2 Inositol 5-Phosphatase Ship1 Is Recruited in an SH2-dependent Manner to the Erythropoietin Receptor
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Identification and Characterization of a Dimerization Domain in CED-6, an Adapter Protein Involved in Engulfment of Apoptotic Cells
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Inositol Phospholipid Signaling and the Biology of Natural Killer Cells
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A Spectrum of Mutations in SH2D1A That Causes X-linked Lymphoproliferative Disease and Other Epstein-Barr Virus-associated Illnesses
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CD94/NKG2-A Inhibitory Complex Blocks CD16-Triggered Syk and Extracellular Regulated Kinase Activation, Leading to Cytotoxic Function of Human NK Cells
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Enzymatic and non-enzymatic activities of SHIP-1 in signal transduction and cancer
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Co‐receptor and accessory regulation of B‐cell antigen receptor signal transduction
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Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes
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Design and Use of an Inducibly Activated Human Immunodeficiency Virus Type 1 Nef To Study Immune Modulation
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Distinct migration patterns of naive and effector CD8 T cells in the spleen: correlation with CCR7 receptor expression and chemokine reactivity
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The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the Dok1 phosphoprotein in Bcr-Abl transformed cells
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The Two SH2-Domain-Containing Inositol 5-Phosphatases SHIP1 and SHIP2 Are Coexpressed in Human T Lymphocytes
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Positive Regulation of Interleukin-4-mediated Proliferation by the SH2-containing Inositol-5′-phosphatase
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Molecular control of PtdIns(3,4,5)P3 signaling in neutrophils
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PIP3 pathway in regulatory T cells and autoimmunity
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Cooperation and selectivity of the two Grb2 binding sites of p52Shc in T-cell antigen receptor signaling to Ras family GTPases and Myc-dependent survival
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Cloning of the Genomic Locus of Mouse SH2 Containing Inositol 5-Phosphatase (SHIP) and a Novel 110-kDa Splice Isoform, SHIPδ
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Positive and Negative Signaling in B Lymphocytes
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The rise and fall of anandamide: processes that control synthesis, degradation, and storage
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HIV‐1 Nef induces p47phox phosphorylation leading to a rapid superoxide anion release from the U937 human monoblastic cell line
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The inositol 5-phosphatase SHIP is expressed as 145 and 135 kDa proteins in blood and bone marrow cells in vivo, whereas carboxyl-truncated forms of SHIP are generated by proteolytic cleavage in vitro
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pp60c-src associates with the SH2-containing inositol-5-phosphatase SHIP1 and is involved in its tyrosine phosphorylation downstream of alphaIIbbeta3 integrin in human platelets.
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The Shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3
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Role of the Src Homology 2 (SH2) Domain and C-Terminus Tyrosine Phosphorylation Sites of SH2-Containing Inositol Phosphatase (SHIP) in the Regulation of Insulin-Induced Mitogenesis
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IL-4 Signaling Is Regulated through the Recruitment of Phosphatases, Kinases, and SOCS Proteins to the Receptor ComplexPreprint
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A Key Role for the Phosphorylation of Ser440 by the Cyclic AMP-dependent Protein Kinase in Regulating the Activity of the Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIP1)
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The Role of the SRC Homology 2-Containing Inositol 5′-Phosphatase in FcɛR1-Induced Signaling
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The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-α interaction
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Complement Receptor 3 Has Negative Impact on Tumor Surveillance through Suppression of Natural Killer Cell Function
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The Tec Kinase–Regulated Phosphoproteome Reveals a Mechanism for the Regulation of Inhibitory Signals in Murine Macrophages
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Role of Shc in T‐cell development and function
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Recombinant p42IP4, a brain‐specific 42‐kDa high‐affinity Ins(1,3,4,5)P4 receptor protein, specifically interacts with lipid membranes containing Ptd‐Ins(3,4,5)P3
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SHIP negatively regulates type II immune responses in mast cells and macrophages
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Regulation of hematopoietic cell signaling by SHIP-1 inositol phosphatase: growth factors and beyond
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INPP5D/SHIP1: Expression, Regulation and Roles in Alzheimer’s Disease Pathophysiology
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Strategy for Leukemia Treatment Targeting SHP-1,2 and SHIP
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The role of SHIP1 in T-lymphocyte life and death
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Different roles of SHIP1 according to the cell context: The example of blood platelets
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A Role for SHIP in Stem Cell Biology and Transplantation
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Tyrosine Phosphorylation of Shc in Response to B Cell Antigen Receptor Engagement Depends on the SHIP Inositol Phosphatase
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FcγRIIB-Independent Mechanisms Controlling Membrane Localization of the Inhibitory Phosphatase SHIP in Human B Cells
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Regulation of the Src Homology 2-containing Inositol 5-Phosphatase SHIP1 in HIP1/PDGFβR-transformed Cells
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The inositol 5-phosphatase SHIP-1 and adaptors Dok-1 and 2 play central roles in CD4-mediated inhibitory signaling
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SHIP1 and the negative control of mast cell/basophil activation by supra-optimal antigen concentrations
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Polyomavirus Middle T Antigen as a Probe for T Cell Antigen Receptor-coupled Signaling Pathways
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Gab Adapter Proteins as Therapeutic Targets for Hematologic Disease
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Mechanism of SHIP-Mediated Inhibition of Insulin- and Platelet-Derived Growth Factor-Stimulated Mitogen-Activated Protein Kinase Activity in 3T3-L1 Adipocytes
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The Src Homology 2-Containing Inositol 5-Phosphatase 1 (SHIP1) is involved in CD32a signaling in human neutrophils
Vaillancourt, M., Levasseur, S., Tremblay, M.-L., Marois, L., Rollet, E., & Naccache, P. H. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.03.012 · Cited by 11 · see citing works
SHIP-mediated inhibition of K562 erythroid differentiation requires an intact catalytic domain and Shc binding site
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Tyrosine Phosphorylation of Shc in Response to B Cell Antigen Receptor Engagement Depends on the SHIP Inositol Phosphatase
Ingham, R. J., Okada, H., Dang-Lawson, M., Dinglasan, J., van der Geer, P., Kurosaki, T., & Gold, M. R. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.11.5891 · Cited by 16 · see citing works
Binding Affinities of Tyrosine-phosphorylated Peptides to the COOH-terminal SH2 and NH2-terminal Phosphotyrosine Binding Domains of Shc
Zhou, M., Harlan, J. E., Wade, W. S., Crosby, S. D., Ravichandran, K. S., Burakoff, S. J., & Fesik, S. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.31119 · Cited by 60 · see citing works
Self-citation
The Src Homology 2 (SH2) Domain of SH2-containing Inositol Phosphatase (SHIP) Is Essential for Tyrosine Phosphorylation of SHIP, Its Association with Shc, and Its Induction of Apoptosis
Liu, L., Damen, J. E., Hughes, M. R., Babić, I., Jirik, F. R., & Krystal, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.8983 · Cited by 119 · see citing works
Self-citation
A Phosphorylation-Dependent Gating Mechanism Controls the SH2 Domain Interactions of the Shc Adaptor Protein
George, R., Schüller, A. C., Harris, R., & Ladbury, J. E. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.040 · Cited by 21 · see citing works
Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling.
Ravichandran, K. S., Igras, V., Shoelson, S. E., Fesik, S. W., & Burakoff, S. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5275 · Cited by 102 · see citing works
Self-citation

Authors: Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G., & Ravichandran, K. S.
Affiliations: University of Virginia (US)
Corresponding author: Krystal, Gerald
ORCID: Lamkin, Thomas D.
Liu, Ling
Krystal, Gerald
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-04
Volume: 272
Issue: 16
Pages: 10396-10401
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.16.10396
OpenAlex: W2056911198
Cited by: 118
References: 50
Citations by year: 2026: 2 · 2023: 2 · 2021: 2 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 1 · 2012: 5
FWCI: 6.28
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8592 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Allergy and Infectious Diseases (AI07496-02, T32AI007496)
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
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Keywords: Shc, ships, phosphotyrosine binding domain, protein-protein interaction, T cell receptor signaling, tyrosine phosphorylation, Lck tyrosine kinase, SH2 domain, adaptor proteins, antigen receptor signaling, cytokine receptor signaling, hematopoietic cells
MeSH terms: Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Amino Acid Sequence, Animals, Binding Sites, Cell Line, Hybridomas, Phosphoric Monoester Hydrolases, Recombinant Fusion Proteins, T-Lymphocytes, Transfection, Mutagenesis, Site-Directed, Point Mutation, src Homology Domains, Phosphotyrosine, COS Cells, Mice

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Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIP

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