Structure, function, and biology of SHIP proteins

PTEN , a Putative Protein Tyrosine Phosphatase Gene Mutated in Human Brain, Breast, and Prostate Cancer

Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., et al. (1997) · Science · doi:10.1126/science.275.5308.1943 · Cited by 4,785

Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

Steck, P. A., Pershouse, M. A., Jasser, S. A., Yung, W. K. A., Lin, H., Ligon, A. H., Langford, L. A., Baumgard, M. L., Hattier, T., Davis, T., et al. (1997) · Nature Genetics · doi:10.1038/ng0497-356 · Cited by 2,742

SH2 domains recognize specific phosphopeptide sequences

Songyang, Z. (1993) · Cell · doi:10.1016/0092-8674(93)90404-e · Cited by 2,620

Signal Transduction through MAP Kinase Cascades

Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759

Targeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease

Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,539

Pten is essential for embryonic development and tumour suppression

Cristofano, A. D., Pesce, B., Cordon‐Cardo, C., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/1235 · Cited by 1,518

Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B

Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061

Specific Inhibition of Stat3 Signal Transduction by PIAS3

Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980

Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases

Rozakis-Adcock, M., McGlade, J. C., Mbamalu, G., Pelicci, G., Daly, R. J., Li, W., Batzer, A., Thomas, S. Μ., Brugge, J. S., Pelicci, P. G., et al. (1992) · Nature · doi:10.1038/360689a0 · Cited by 973

Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems

Podsypanina, K., Ellenson, L. H., Nemes, A., Gu, J., Tamura, M., Yamada, K. M., Cordon‐Cardo, C., Cattoretti, G., Fisher, P. E., & Parsons, R. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1563 · Cited by 947

SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signalling motif

Pesesse, X., Backers, K., Moreau, C., Zhang, J., Bléro, D., Paternotte, N., & Erneux, C. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.013 · Cited by 15

Pore-forming proteins and their role in cancer and inflammation: Mechanistic insights and plausible druggable targets

Sankar, J., Arora, S., Joshi, G., & Kumar, R. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110127 · Cited by 14

The SH2-containing inositol 5-phosphatase (SHIP)-1 is implicated in the control of cell-cell junction and induces dissociation and dispersion of MDCK cells

Mancini, A., Koch, A., Wilms, R., & Tamura, T. (2002) · Oncogene · doi:10.1038/sj.onc.1205224 · Cited by 14

Gene transfer of SHIP-1 inhibits proliferation of juvenile myelomonocytic leukemia cells carrying KRAS2 or PTPN11 mutations

Metzner, A., Horstmann, M. A., Fehse, B., Ortmeyer, G., Niemeyer, C. M., Stocking, C., Mayr, G. W., & Jücker, M. (2007) · Gene Therapy · doi:10.1038/sj.gt.3302912 · Cited by 14

Tribbles Pseudokinase 2 (TRIB2) Regulates Expression of Binding Partners in Bovine Granulosa Cells

Warma, A., Lussier, J. G., & Ndiaye, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041533 · Cited by 13

Nuclear accumulation of SHIP1 mutants derived from AML patients leads to increased proliferation of leukemic cells

Nalaskowski, M. M., Ehm, P. A. H., Rehbach, C., Nelson, N., Täger, M., Modest, K., & Jücker, M. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.05.006 · Cited by 11

SHIP1 and the negative control of mast cell/basophil activation by supra-optimal antigen concentrations

Huber, M., & Gibbs, B. F. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.02.017 · Cited by 13

Signaling by ITIM-Bearing Receptors

Verbrugge, A., & Meyaard, L. (2005) · Current Immunology Reviews · doi:10.2174/1573395054065160 · Cited by 13

p66Shc Is a Negative Regulator of FcεRI-Dependent Signaling in Mast Cells

Ulivieri, C., Fanigliulo, D., Masi, G., Savino, M. T., Gamberucci, A., Pelicci, P. G., & Baldari, C. T. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001391 · Cited by 12

PI3Ks—Drug Targets in Inflammation and Cancer

Wymann, M. P. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-3012-0_5 · Cited by 11

Mechanism of SHIP-Mediated Inhibition of Insulin- and Platelet-Derived Growth Factor-Stimulated Mitogen-Activated Protein Kinase Activity in 3T3-L1 Adipocytes

Sharma, P. M., Son, H.-S., Ugi, S., Ricketts, W., & Olefsky, J. M. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0096 · Cited by 10

Repression of RIPK1 kinase by INPP5D inhibits expression of diverse proinflammatory mediators and late-onset Alzheimer’s disease risk factors

Xie, X., Liu, J., Liang, W., Zhang, Y., Gong, X., Yuan, S., Qi, C., Huang, M., Shi, L., Hou, M., et al. (2026) · Immunity · doi:10.1016/j.immuni.2026.01.014 · Cited by 10

Deficiency of Lipid Phosphatase SHIP Enables Long-Term Reconstitution of Hematopoietic Inductive Bone Marrow Microenvironment

Liang, O. D., Lu, J., Nombela‐Arrieta, C., Jia, Z., Zhao, L., Pivarnik, G., Mondal, S., Chai, L., Silberstein, L. E., & Luo, H. R. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.04.016 · Cited by 10

Biochemistry and structure of phosphoinositide phosphatases

Kim, Y. J., Jahan, N., & Bahk, Y. Y. (2013) · BMB Reports · doi:10.5483/bmbrep.2013.46.1.261 · Cited by 10

Lipid phosphatase SHIP‐1 regulates chondrocyte hypertrophy and skeletal development

So, E. Y., Sun, C., Wu, K. Q., Driesman, A. S., Leggett, S. E., Isaac, M., Spangler, T., Dubielecka, P. M., Reginato, A. M., & Liang, O. D. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29063 · Cited by 7

Activated Src kinases downstream of BCR-ABL and Flt3 induces proteasomal degradation of SHIP1 by phosphorylation of tyrosine 1021

Ehm, P. A. H., Bettin, B., & Jücker, M. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119467 · Cited by 9

Introduction: multifaceted roles of lipids and their catabolites in immune cell signaling

Ott, V. L., & Cambier, J. C. (2002) · Seminars in Immunology · doi:10.1006/smim.2001.0336 · Cited by 9

INPP5D/SHIP1 regulates inflammasome activation in human microglia

Chou, V., Fancher, S. B., Pearse, R. V., Lee, H., Lam, M., Seyfried, N. T., Bennett, D. A., De Jager, P. L., Menon, V., & Young-Pearse, T. L. (2023) · doi:10.1101/2023.02.25.530025 · Cited by 8

JAK2-V617F is a negative regulation factor of SHIP1 protein and thus influences the AKT signaling pathway in patients with Myeloproliferative neoplasm (MPN)

Glück, M., Dally, L., Jücker, M., & Ehm, P. A. H. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106229 · Cited by 8

History of Histamine-Releasing Factor (HRF)/Translationally Controlled Tumor Protein (TCTP) Including a Potential Therapeutic Target in Asthma and Allergy

MacDonald, S. M. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-67591-6_16 · Cited by 8

New insights into Dok-4 PTB domain structure and function

Hooker, E., Baldwin, C., & Lemay, S. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.08.148 · Cited by 8

Purification and Identification of Protein-Tyrosine Kinase-binding Proteins Using Synthetic Phosphopeptides as Affinity Reagents

Wilhelmsen, K., Copp, J., Glenn, G. M., Hoffman, R. C., Tucker, P. W., & van der Geer, P. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400062-mcp200 · Cited by 6

p135 Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIPβ) Isoform Can Substitute for p145 SHIP in FcγRIIB1-mediated Inhibitory Signaling in B Cells

March, M., Lucas, D. M., Aman, M. J., & Ravichandran, K. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003714200 · Cited by 6

Inhibiting phosphatase SHIP-1 enhances suboptimal IgE-mediated activation of human blood basophils but inhibits IgE-mediated activation of cultured human mast cells

Rasmussen, P., Spillner, E., & Hoffmann, H. J. (2019) · Immunology Letters · doi:10.1016/j.imlet.2019.04.003 · Cited by 5

SHIP1 Controls Internal Platelet Contraction and αIIbβ3 Integrin Dynamics in Early Platelet Activation

Séverin, S., Consonni, A., Chicanne, G., Allart, S., Payrastre, B., & Gratacap, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020958 · Cited by 5

Profiling of Phosphatidylinositol 3-Kinase (PI3K) Proteins in Insulin Signaling Pathway

Chakraborty, C., Doss, C. G. P., Bhatia, R., & Agoramoorthy, G. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1515-4 · Cited by 6

The Src Homology 2 Containing Inositol 5′ Phosphatases

Antignano, F., Rüschmann, J., Hamilton, M. J., Ho, V. W., Lam, V., Kuroda, E., Sly, L. M., & Krystal, G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00134-0 · Cited by 4

Pathological Roles of INPP5D in Alzheimer’s Disease

Chu, Y. N., Akahori, A., Takatori, S., & Tomita, T. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-31978-5_30 · Cited by 3

PI3K Is a Linker Between L-selectin and PSGL-1 Signaling to IL-18 Transcriptional Activation at the Promoter Level

Luo, J. (2017) · Inflammation · doi:10.1007/s10753-017-0711-5 · Cited by 3

Two Diseases with One Hit: Inhibiting a Potential Diabetes Target to Reduce Cancer Risk and to Improve Anti-Cancer Therapy

Prasad, N. K. (2009) · Current Cancer Therapy Reviews · doi:10.2174/157339409788166779 · Cited by 3

Regulation of FcεRI Signaling by Lipid Phosphatases

Kuhny, M., Zorn, C. N., & Huber, M. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-07911-0_6 · Cited by 3

The PI3K signaling pathway; from normal lymphopoiesis to lymphoid malignancies

Kashani, B., Zandi, Z., Pourbagheri‐Sigaroodi, A., Yousefi, A., Ghaffari, S. H., & Bashash, D. (2024) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2024.2350629 · Cited by 2

Accumulation of Splice Variants and Transcripts in Response to PI3K Inhibition in T Cells

Riedel, A., Mofolo, B., Avota, E., Schneider‐Schaulies, S., Meintjes, A., Mulder, N., & Kneitz, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0050695 · Cited by 2

Study of SHIP‐binding cell surface proteins suggests c‐kit as a SHIP‐interacting receptor in mast cells

Ott, V. L., Moffitt, L. A., & Cambier, J. C. (2005) · Signal Transduction · doi:10.1002/sita.200400029 · Cited by 2

Lipid Mediated Regulation of Protein Kinases

Pandit, S., & Mishra, G. (2020) · Wiley eBooks · doi:10.1002/9781119541578.ch7 · Cited by 2

Emerging oral Treponema membrane proteins disorder neutrophil phosphoinositide signaling via phosphatidylinositol-4-phosphate 5-kinase

Anselmi, N. K., Vanyo, S. T., & Visser, M. B. (2025) · Frontiers in Oral Health · doi:10.3389/froh.2025.1568983 · Cited by 1

The power of five – inositol polyphosphate 5‐phosphatase gene mutations at the intersection of development and disease

McGrath, M. J., Davies, E. M., Ooms, L. M., Nanayakkara, R., Gurung, R., Jones, E. I., & Mitchell, C. A. (2025) · FEBS Letters · doi:10.1002/1873-3468.70247 · Cited by 1

Roles of HTLV-1 Tax in Leukemogenesis of Human T-Cells

Mizuguchi, M., Hara, T., & Nakamur, M. (2011) · InTech eBooks · doi:10.5772/22254 · Cited by 1

Mechanisms of Hdac2 function in the regulation of adult cardiac hypertrophy and embryonic myocyte proliferation

Zhu, W. (2010) · ScholarlyCommons (University of Pennsylvania) · Cited by 1

Identification of SHIP-1 and SHIP-2 homologs in channel catfish, Ictalurus punctatus

Taylor, E. B., Nayak, D. K., Quiniou, S. M. A., Bengtén, E., & Wilson, M. (2015) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2015.02.015 · Cited by 1

Histamine Releasing Factor/Translationally Controlled Tumor Protein: History, Functions and Clinical Implications

MacDonald, S. M. (2012) · The Open Allergy Journal · doi:10.2174/1874838401205010012 · Cited by 1

SH2-Containing Inositol 5′-Phosphatase Inhibits Transformation of Abelson Murine Leukemia Virus

Fessler, S. P., Rosenberg, N. E., & Baughn, L. B. (2011) · Journal of Virology · doi:10.1128/jvi.05115-11 · Cited by 1

Phosphoinositide 3-Kinases

Fruman, D. A. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50507-6 · Cited by 1

PNH: “plus ca change, plus c'est la meme chose”

Parker, C. J. (2002) · Blood · doi:10.1182/blood.v99.1.2 · Cited by 1

The role of SHIP1 in modulating disease severity in the K/BxN serum transfer model of rheumatoid arthritis

Hirukawa, A. (2011) · cIRcle (University of British Columbia) · doi:10.14288/1.0072036 · Cited by 1

SHIP Inositol Phosphate Phosphatases

Rohrschneider, L. R. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50509-x · Cited by 1

La régulation du métabolisme du glucose par la protéine tyrosine phosphatase SHP-1

Bergeron, S. (2007) · Corpus Université Laval (Université Laval) · Cited by 1

A role for the SH2-containing inositol phosphatase in the biology of natural killer cells and stem cells

Ghansah, T., Ninos, J. M., & Kerr, W. G. (2001) · Springer eBooks · doi:10.1007/978-4-431-53940-7_17

SHIP and Tumour-Associated Macrophages

Ho, V. W., Hamilton, M. J., Kuroda, E., Rüschmann, J., Antignano, F., Lam, V., & Krystal, G. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0662-4_10

Bayesian microarray one-way anova and grouping cell lines by equal expression levels

Lönnstedt, I. M., & Rimini, R. (2004)

Tumor Suppressor Role of Abl Kinase in CrkI-Transformed Fibroblasts and Its Implication in Human Cancer Cells

Ng, K. Y. (2015) · OpenCommons - UConn (University of Connecticut)

Untersuchungen zur Funktion des PI3K/Akt-Signalweges für das Wachstum von disseminierten Tumorzelllinien von Patienten mit Malignomen

Grupp, K. (2013)

Studies into the function and regulation of SHIP

Rüschmann, J. (2009) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-7073

Mechanisms of LAIR-1 mediated inhibition of immune function

Verbrugge, A. (2005) · Utrecht University Repository (Utrecht University)

Microarray analysis of differentially regulated genes in human leukemia cells after expression of the inositol 5-phosphatase SHIP

Palma, G., & Elena, L. (2006)

Role of phosphoinositide 3-kinases in mast cell activation

Collmann, E. (2009) · edoc (University of Basel) · doi:10.5451/unibas-004970278

Efeito do fluoreto no osso de camundongos com diferentes susceptibilidades genéticas à fluorose: uma análise proteômica

Kobayashi, C. A. N. (2012) · doi:10.11606/t.25.2012.tde-02102012-104045

Inositol Phospholipid and Tyrosine Phosphorylation Signaling in the Biology of Hematopoietic Stem Cells

Hazen, A. L. (2009) · Digital Commons - University of South Florida (University of South Florida)

The role of the "Yaa (Y-linked autoimmune acceleration)" mutation and the Fc gamma receptor type IIB (FcγRIIB) in the control of lupus-like autoimmune responses in mice

Moll, T. (2004) · Archive ouverte UNIGE (University of Geneva) · doi:10.13097/archive-ouverte/unige:306

Signaling in natural killer cells: SHIP, 2B4 and the Kinome

Wahle, J. A. (2007) · Digital Commons - University of South Florida (University of South Florida)

The role of Src homology 2 domain containing 5' inositol phosphatase 1 (SHIP) in hematopoietic cells

Desponts, C. (2006) · Digital Commons - University of South Florida (University of South Florida)

Regulation of effector/memory T cell activation by inducible co-stimulator (ICOS).

Franko, J. (2009) · OhioLink ETD Center (Ohio Library and Information Network)

The Role of the Forkhead Transcription Factor Foxo3a in Erythropoiesis

Bakker, W. J. (2005)

Investigating the isoform-specific role of phosphoinositide 3- kinase p110delta

Nock, G. E. (2008) · UCL Discovery (University College London)

Myeloproliferation or dysplasia: a matter of PIP3 levels?

Glimm, H. (2004) · Blood · doi:10.1182/blood-2004-04-1268

Intracellular signaling of phosphorylated insitol compounds : A study in pancreatic beta-cells and hippocampal neurons

Yu, J. H. (2004) · Figshare

Phosphoinositide 3-kinase (PI3K) as a New Therapeutic Target for Rheumatoid Arthritis

Kim, H. (2013) · Journal of Rheumatic Diseases · doi:10.4078/jrd.2013.20.2.74

Mind Your Xs and Ys: Genetics of the Autoimmune Disease Systemic Lupus Erythematosus

Crampton, S. P., & Bolland, S. M. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-512-5_37

Signal Inhibitory Receptor on Leukocytes-1 (SIRL-1), a potent regulator of neutrophil function

Avondt, K. V. (2014) · Utrecht University Repository (Utrecht University)

Allogeneic Effector Cell Populations

Verneris, M. R., & Negrin, R. S. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-333-0_25

Src homology 2 domain-containing inositol-5’ phosphatase in a murine model of Amyotrophic Lateral Sclerosis

Parrott, H. A. (2009) · Summit (Simon Fraser University)

The role of SHIP in dendritic cell differentiation and function

Antignano, F. (2009) · cIRcle (University of British Columbia) · doi:10.14288/1.0067312

The Role of CCL5/CCR5 Signal Transduction in T cell Function and Breast Cancer

Murooka, T. T. (2009) · TSpace (University of Toronto)

Intracellular Signaling Networks in the Immune Response: Pathways Activated by Interleukin-2 and-4 Receptors and Their Roles in T Cell Proliferation

Comfort, K. K. (2006)

Signaling Pathways Activated by Interleukin-2 and Interluekin-4 Receptors Mediate T Lymphocyte Clonal Expansion

Comfort, K. K. (2007)

Investigating the roles of two key negative regulators of the PI3K pathway in T cell-mediated autoimmunity

Johnson, T. (2007) · doi:10.11575/prism/11212

A Novel Therapeutic Approach in Breast and Hematopoietic Cancers: Inhibition of SH2-Domain Containing Inositol 5' Phosphatase (SHIP)

Balch, A. (2013) · Syracuse University Libraries (Syracuse University)

Allogeneic Effector Cell Populations: Separating GVL from GVHD

Verneris, M. R., & Negrin, R. S. (2003) · Humana Press eBooks · doi:10.1385/1-59259-333-x:387

Determining Lineage Fate, Survival and Proliferation of Differentiating Thymocytes: Interplay between Notch, TCR, PI3K and MAPK Pathways

Wong, G. W. (2013) · TSpace (University of Toronto)

Role of SHIP-1 phosphatase in trained immunity modulation

Sanz-Leal, P. (2018) · doi:10.4321/repisalud.7167

Calcium, Calmodulin, and Phospholipids

Bolander, F. F. (2004) · Elsevier eBooks · doi:10.1016/b978-012111232-5/50010-5

PKB/Akt : a critical regulator of lymphocyte, development and function

Na, S. (2005)

Pro and Anti Tumorigenic Effects of EPHA Receptor Signaling in Breast and Lung Cancer

Zhuang, G. (2010)

Inactivation of SHIP1 in acute lymphoblastic leukemia

Lo, T. C. T. (2009) · eScholarship (California Digital Library)

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The SHIP1-inflammatory-lipid axis in Alzheimer’s disease: from genetic risk to spatiotemporal mechanistic insights

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INPP5D/SHIP1 in Alzheimer’s Disease: Linking Microglial Substrate Handling to Neuroinflammation and Neurovascular Dysfunction

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