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Molecular and Cellular Biology Volume 19, 1999 - Issue 11
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Cell Growth and Development

BCR/ABL Directly Inhibits Expression of SHIP, an SH2-Containing Polyinositol-5-Phosphatase Involved in the Regulation of Hematopoiesis

Martin Sattler1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115Correspondence[email protected]
,
Shalini Verma1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115
,
Christopher H. Byrne1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115
,
Gautam Shrikhande1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115
,
Thomas Winkler1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115
,
Paul A. Algate2 Department of Basic Science, Fred Hutchinson Cancer Research Center, Seattle, Washington98109
,
Larry R. Rohrschneider2 Department of Basic Science, Fred Hutchinson Cancer Research Center, Seattle, Washington98109
&
James D. Griffin1 Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts02115
 show all
Pages 7473-7480 | Received 20 May 1999, Accepted 16 Aug 1999, Published online: 28 Mar 2023

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Patrick Ehm, Marcus M Nalaskowski, Torsten Wundenberg & Manfred Jücker. (2015) The tumor suppressor SHIP1 colocalizes in nucleolar cavities with p53 and components of PML nuclear bodies. Nucleus 6:2, pages 154-164.
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Articles from other publishers (81)

Patrick Ehm, Bettina Bettin & Manfred Jücker. (2023) Activated Src kinases downstream of BCR-ABL and Flt3 induces proteasomal degradation of SHIP1 by phosphorylation of tyrosine 1021. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1870:5, pages 119467.
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Patrick Ehm, Nina Nelson, Susanne Giehler, Matthias Schaks, Bettina Bettin, Johannes Kirchmair & Manfred Jücker. (2023) Reduced expression and activity of patient-derived SHIP1 phosphatase domain mutants. Cellular Signalling 101, pages 110485.
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Madeleine Glück, Lina Dally, Manfred Jücker & Patrick Ehm. (2022) JAK2-V617F is a negative regulation factor of SHIP1 protein and thus influences the AKT signaling pathway in patients with Myeloproliferative neoplasm (MPN). The International Journal of Biochemistry & Cell Biology 149, pages 106229.
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Lauren M. Brown, Soroor Hediyeh-zadeh, Teresa SadrasHannah HuckstepJarrod J. SandowRay C. BartoloHansen J. Kosasih, Nadia M. DavidsonBreon SchmidtStefan Bjelosevic, Ricky JohnstoneAndrew I. Webb, Seong L. Khaw, Alicia Oshlack, Melissa J. Davis & Paul G. Ekert. (2022) SFPQ-ABL1 and BCR-ABL1 use different signaling networks to drive B-cell acute lymphoblastic leukemia. Blood Advances 6:7, pages 2373-2387.
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Jevon A. Cutler, Savita Udainiya, Anil K. Madugundu, Santosh Renuse, Yaoyu Xu, Jaehun Jung, Kwang Pyo Kim, Xinyan Wu & Akhilesh Pandey. (2019) Integrative phosphoproteome and interactome analysis of the role of Ubash3b in BCR-ABL signaling. Leukemia 34:1, pages 301-305.
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Shrinidh Joshi & Yagna P R Jarajapu. (2018) Mitochondrial depolarization stimulates vascular repair‐relevant functions of CD34 + cells via reactive oxygen species‐induced nitric oxide generation . British Journal of Pharmacology 176:22, pages 4373-4387.
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Patrick A.H. Ehm, Fabiola Lange, Carolin Hentschel, Anneke Jepsen, Madeleine Glück, Nina Nelson, Bettina Bettin, Christina de Bruyn Kops, Johannes Kirchmair, Marcus Nalaskowski & Manfred Jücker. (2019) Analysis of the FLVR motif of SHIP1 and its importance for the protein stability of SH2 containing signaling proteins. Cellular Signalling 63, pages 109380.
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Lindsay M. Gurska, Kristina Ames & Kira Gritsman. 2019. Leukemia Stem Cells in Hematologic Malignancies. Leukemia Stem Cells in Hematologic Malignancies 1 39 .
Marcus M. Nalaskowski, Patrick Ehm, Christoph Rehbach, Nina Nelson, Maike Täger, Kathrin Modest & Manfred Jücker. (2018) Nuclear accumulation of SHIP1 mutants derived from AML patients leads to increased proliferation of leukemic cells. Cellular Signalling 49, pages 87-94.
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Peter Dobranowski & Laura M Sly. (2018) SHIP negatively regulates type II immune responses in mast cells and macrophages. Journal of Leukocyte Biology 103:6, pages 1053-1064.
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Helena Brauer, Julia Strauss, Wiebke Wegner, Carsten Müller-Tidow, Martin Horstmann & Manfred Jücker. (2012) Leukemia-associated mutations in SHIP1 inhibit its enzymatic activity, interaction with the GM-CSF receptor and Grb2, and its ability to inactivate PI3K/AKT signaling. Cellular Signalling 24:11, pages 2095-2101.
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D W Lee, M Futami, M Carroll, Y Feng, Z Wang, M Fernandez, Z Whichard, Y Chen, S Kornblau, E J Shpall, C E Bueso-Ramos & S J Corey. (2012) Loss of SHIP-1 protein expression in high-risk myelodysplastic syndromes is associated with miR-210 and miR-155. Oncogene 31:37, pages 4085-4094.
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Marcus M. Nalaskowski, Anja Metzner, Maria A. Brehm, Sena Labiadh, Helena Brauer, Nicole Grabinski, Georg W. Mayr & Manfred Jücker. (2012) The inositol 5-phosphatase SHIP1 is a nucleo-cytoplasmic shuttling protein and enzymatically active in cell nuclei. Cellular Signalling 24:3, pages 621-628.
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