Posttranscriptional regulation of the p85α.alpha; adapter subunit of phosphatidylinositol 3-kinase in human leukemia cells

References

• Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002;296:1655–1657.
   PubMed Web of Science ®Google Scholar
• Aoki M, Batista O, Bellacosa A, Tsichlis P, Vogt PK. The akt kinase: molecular determinants of oncogenicity. Proc Natl Acad Sci USA 1998;95:14950–14955.
   PubMed Web of Science ®Google Scholar
• Min YH, Eom JI, Cheong JW, et al. Constitutive phosphorylation of Akt/PKB protein in acute myeloid leukemia: its significance as a prognostic variable. Leukemia 2003;17:995–997.
   PubMed Web of Science ®Google Scholar
• Martelli AM, Nyakern M, Tabellini G, et al. Phosphoinositide 3-kinase/Akt signaling pathway and its therapeutical implications for human acute myeloid leukemia. Leukemia 2006;20:911–928.
   PubMed Web of Science ®Google Scholar
• Deane JA, Fruman DA. Phosphoinositide 3-kinase: diverse roles in immune cell activation. Annu Rev Immunol 2004;22:563–598.
   PubMed Web of Science ®Google Scholar
• Okkenhaug K, Vanhaesebroeck B. New responsibilities for the PI3K regulatory subunit p85 alpha. Sci STKE 2001;2001(76):pe1.
   PubMedGoogle Scholar
• Yu J, Zhang Y, McIlroy J, Rordorf-Nikolic T, Orr GA, Backer JM. Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110alpha catalytic subunit by the p85 regulatory subunit. Mol Cell Biol 1998;18:1379–1387.
   PubMed Web of Science ®Google Scholar
• Ueki K, Fruman DA, Brachmann SM, Tseng YH, Cantley LC, Kahn CR. Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival. Mol Cell Biol 2002;22:965–977.
   PubMed Web of Science ®Google Scholar
• Inoue G, Cheatham B, Emkey R, Kahn CR. Dynamics of insulin signaling in 3T3-L1 adipocytes. Differential compartmentalization and trafficking of insulin receptor substrate (IRS)- 1 and IRS-2. J Biol Chem 1998;273:11548–11555.
   PubMed Web of Science ®Google Scholar
• Luo J, Field SJ, Lee JY, Engelman JA, Cantley LC. The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex. J Cell Biol 2005;170:455–464.
   PubMedGoogle Scholar
• Taniguchi CM, Tran TT, Kondo T, et al. Phosphoinositide 3-kinase regulatory subunit p85alpha suppresses insulin action via positive regulation of PTEN. Proc Natl Acad Sci USA 2006;103:12093–12097.
   PubMed Web of Science ®Google Scholar
• Hoxha E, Fehse B, Ortmeyer G, Stocking C, Mayr GW, Jucker M. Overexpression of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase inhibits GM-CSF-dependent colony formation of CD34+ hematopoietic progenitor cells. Leuk Lymphoma 2008;49:1206–1208.
   PubMed Web of Science ®Google Scholar
• Samuels Y, Wang Z, Bardelli A, et al. High frequency of mutations of the PIK3CA gene in human cancers. Science 2004;304:554.
   PubMed Web of Science ®Google Scholar
• Philp AJ, Campbell IG, Leet C, et al. The phosphatidylinositol 3′-kinase p85alpha gene is an oncogene in human ovarian and colon tumors. Cancer Res 2001;61:7426–7429.
   PubMed Web of Science ®Google Scholar
• Shi BH, Nashimoto T, Andoh R, et al. Mutation of the PI3′ kinase gene in a human colon carcinoma cell line, HCC2998. DNA Cell Biol 2006;25:399–405.
   PubMed Web of Science ®Google Scholar
• Cancer Genome Atlas Research Network. Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 2008;455:1061–1068.
   PubMed Web of Science ®Google Scholar
• Jaiswal BS, Janakiraman V, Kljavin NM, et al. Somatic mutations in p85alpha promote tumorigenesis through class IA PI3K activation. Cancer Cell 2009;16:463–474.
   PubMed Web of Science ®Google Scholar
• Horn S, Bergholz U, Jucker M, et al. Mutations in the catalytic subunit of class IA PI3K confer leukemogenic potential to hematopoietic cells. Oncogene 2008;27:4096–4106.
   PubMed Web of Science ®Google Scholar
• Jimenez C, Jones DR, Rodriguez-Viciana P, et al. Identification and characterization of a new oncogene derived from the regulatory subunit of phosphoinositide 3-kinase. EMBO J 1998;17:743–753.
   PubMed Web of Science ®Google Scholar
• Borlado LR, Redondo C, Alvarez B, et al. Increased phosphoinositide 3-kinase activity induces a lymphoproliferative disorder and contributes to tumor generation in vivo. FASEB J 2000;14:895–903.
   PubMed Web of Science ®Google Scholar
• Jucker M, Sudel K, Horn S, et al. Expression of a mutated form of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase in a Hodgkin's lymphoma-derived cell line (CO). Leukemia 2002;16:894–901.
   PubMed Web of Science ®Google Scholar
• Sanger F. Determination of nucleotide sequences in DNA. Science 1981;214:1205–1210.
   PubMed Web of Science ®Google Scholar
• Horn S, Endl E, Fehse B, Weck MM, Mayr GW, Jucker M. Restoration of SHIP activity in a human leukemia cell line downregulates constitutively activated phosphatidylinositol 3-kinase/Akt/GSK-3beta signaling and leads to an increased transit time through the G1 phase of the cell cycle. Leukemia 2004;18:1839–1849.
   Google Scholar
• Garcia-Palma L, Horn S, Haag F, et al. Up-regulation of the T cell quiescence factor KLF2 in a leukaemic T-cell line after expression of the inositol 5′-phosphatase SHIP-1. Br J Haematol 2005;131:628–631.
   PubMed Web of Science ®Google Scholar
• Mohr E, Morris JF, Richter D. Differential subcellular mRNA targeting: deletion of a single nucleotide prevents the transport to axons but not to dendrites of rat hypothalamic magnocellular neurons. Proc Natl Acad Sci USA 1995;92:4377–4381.
   PubMed Web of Science ®Google Scholar
• Horn S, Meyer J, Heukeshoven J, et al. 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. Leukemia 2001;15:112–120.
   PubMed Web of Science ®Google Scholar
• Jucker M, Schiffer CA, Feldman RA. A tyrosine-phosphorylated protein of 140 kD is constitutively associated with the phosphotyrosine binding domain of Shc and the SH3 domains of Grb2 in acute myeloid leukemia cells. Blood 1997;89:2024–2035.
   PubMed Web of Science ®Google Scholar
• Areces LB, Jucker M, San Miguel JA, Mui A, Miyajima A, Feldman RA. Ligand-dependent transformation by the receptor for human granulocyte/macrophage colony-stimulating factor and tyrosine phosphorylation of the receptor beta subunit. Proc Natl Acad Sci USA 1993;90:3963–3967.
   PubMed Web of Science ®Google Scholar
• Wilhelm JE, Smibert CA. Mechanisms of translational regulation in Drosophila. Biol Cell 2005;97:235–252.
   PubMed Web of Science ®Google Scholar
• Furuyama K, Kaneko K, Vargas PD. Heme as a magnificent molecule with multiple missions: heme determines its own fate and governs cellular homeostasis. Tohoku J Exp Med 2007;213:1–16.
   PubMed Web of Science ®Google Scholar
• Anderson P, Kedersha N. Stress granules: the Tao of RNA triage. Trends Biochem Sci 2008;33:141–150.
   PubMed Web of Science ®Google Scholar
• Olsen PH, Ambros V. The lin-4 regulatory RNA controls developmental timing in Caenorhabditis elegans by blocking LIN-14 protein synthesis after the initiation of translation. Dev Biol 1999;216:671–680.
   PubMed Web of Science ®Google Scholar
• Kaspar RL, Gehrke L. Peripheral blood mononuclear cells stimulated with C5a or lipopolysaccharide to synthesize equivalent levels of IL-1 beta mRNA show unequal IL-1 beta protein accumulation but similar polyribosome profiles. J Immunol 1994;153:277–286.
   PubMed Web of Science ®Google Scholar
• Clark IE, Wyckoff D, Gavis ER. Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism. Curr Biol 2000;10:1311–1314.
   PubMedGoogle Scholar
• Braat AK, Yan N, Arn E, Harrison D, Macdonald PM. Localization-dependent oskar protein accumulation; control after the initiation of translation. Dev Cell 2004;7:125–131.
   PubMed Web of Science ®Google Scholar
• Theodorakis NG, Banerji SS, Morimoto RI. HSP70 mRNA translation in chicken reticulocytes is regulated at the level of elongation. J Biol Chem 1988;263:14579–14585.
   PubMed Web of Science ®Google Scholar
• Gross MK, Merrill GF. Thymidine kinase synthesis is repressed in nonreplicating muscle cells by a translational mechanism that does not affect the polysomal distribution of thymidine kinase mRNA. Proc Natl Acad Sci USA 1989;86:4987–4991.
   PubMed Web of Science ®Google Scholar
• Sivan G, Kedersha N, Elroy-Stein O. Ribosomal slowdown mediates translational arrest during cellular division. Mol Cell Biol 2007;27:6639–6646.
   PubMed Web of Science ®Google Scholar
• Shyu AB, Wilkinson MF, van Hoof A. Messenger RNA regulation: to translate or to degrade. EMBO J 2008;27:471–481.
   PubMed Web of Science ®Google Scholar
• Griffiths-Jones S, Saini HK, van Dongen S, Enright AJ. miRBase: tools for microRNA genomics. Nucleic Acids Res 2008;36:D154–D158.
   PubMed Web of Science ®Google Scholar
• Bartel DP. MicroRNAs: target recognition and regulatory functions. Cell 2009;136:215–233.
   PubMed Web of Science ®Google Scholar
• Roques M, Vidal H. A phosphatidylinositol 3-kinase/p70 ribosomal S6 protein kinase pathway is required for the regulation by insulin of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase gene expression in human muscle cells. J Biol Chem 1999;274:34005–34010.
   PubMed Web of Science ®Google Scholar
• del Rincon JP, Iida K, Gaylinn BD, et al. Growth hormone regulation of p85alpha expression and phosphoinositide 3-kinase activity in adipose tissue: mechanism for growth hormone-mediated insulin resistance. Diabetes 2007;56:1638–1646.
   PubMed Web of Science ®Google Scholar
• Foukas LC, Beeton CA, Jensen J, Phillips WA, Shepherd PR. Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo. Mol Cell Biol 2004;24:966–975.
   PubMed Web of Science ®Google Scholar
• Fang D, Wang HY, Fang N, Altman Y, Elly C, Liu YC. Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. J Biol Chem 2001;276:4872–4878.
   PubMed Web of Science ®Google Scholar
• Geering B, Cutillas PR, Nock G, Gharbi SI, Vanhaesebroeck B. Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers. Proc Natl Acad Sci USA 2007;104:7809–7814.
   PubMed Web of Science ®Google Scholar