NDLI: Regulation of the Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIP1) by the Cyclic AMP-dependent Protein Kinase

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Regulation of the Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIP1) by the Cyclic AMP-dependent Protein Kinase

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Regulation of the Src Homology 2 Domain-containing Inositol 5′-Phosphatase (SHIP1) by the Cyclic AMP-dependent Protein Kinase

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Walk, Scott F. Ravichandran, Kodi S. Zhang, Jun Garrison, James C.
Description	Author Affiliation: Zhang J ( Department of Pharmacology, University of Virginia, Charlottevilles, Virginia 22908, USA.)
Abstract	Many agents that activate hematopoietic cells use phos pha tidyl ino si tol 3,4,5-trisphosphate (PtdIns 3,4,5-P(3)) to initiate signaling cascades. The SH2 domain-containing inositol 5' phosphatase, SHIP1, regulates hematopoietic cell function by opposing the action of phos pha tidyl ino si tol 3-kinase and reducing the levels of PtdIns 3,4,5-P(3). Activation of the cyclic AMP-de pend ent protein kinase (PKA) also opposes many of the pro-inflammatory responses of hematopoietic cells. We tested to see whether the activity of SHIP1 was regulated via phos pho ryl a tion with PKA. We prepared pure recombinant SHIP1 from HEK-293 cells and found it can be rapidly phos pho ryl a ted by PKA to a stoichiometry of 0.6 mol of PO(4)/mol of SHIP1. In (32)P-labeled HEK-293 cells transfected with SHIP1, stimulation with Sp-adenosine 3',5'-cyclic monophosphorothioate triethylammonium salt hydrate (Sp-cAMPS) or activation of the beta-adrenergic receptor increased the phos pho ryl a tion state of SHIP1. Inhibition of protein phosphatase activity with okadaic acid also increased the phos pho ryl a tion of SHIP1. Phosphorylation of SHIP1 in vitro or in cells by PKA increased the 5' phosphatase activity of SHIP1 by 2-3-fold. Elevation of Ca(2+) in DT40 cells in response to B cell receptor cross-linking, an indicator of PtdIns 3,4,5-P(3) levels, was markedly blunted by pretreatment with Sp-cAMPS. This effect was absent in SHIP(-/-) DT40 cells showing that the effect of Sp-cAMPS in DT40 cells is SHIP1-de pend ent. Sp-cAMPS also blunted the ability of the B cell receptor to increase the phos pho ryl a tion of Akt in DT40 and A20 cells. Overall, activation of G protein-coupled receptors that raise cyclic AMP cause SHIP1 to be phosphorylated and stimulate its inositol phosphatase activity. These results outline a novel mechanism of SHIP1 regulation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-07-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cyclic AMP-Dependent Protein Kinases Metabolism Phosphoric Monoester Hydrolases Genetics Animals B-Lymphocytes Cell Line Cell Line, Tumor Cyclic AMP Analogs & Derivatives Gene Expression Kidney Cytology Lymphoma, B-Cell Mice Chemistry Isolation & Purification Phosphorylation Protein Phosphatase 1 Receptors, Adrenergic, Beta Recombinant Proteins Thionucleotides Src Homology Domains Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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