Shp2 as a therapeutic target for leptin resistance and obesity

Bibliography

• KOPELMAN PG: Obesity as a medical problem. Nature (2000) 404(6778):635-643.
   PubMed Web of Science ®Google Scholar
• FRIEDMAN JM: Modern science versus the stigma of obesity. Nat. Med. (2004) 10(6):563-569.
   PubMed Web of Science ®Google Scholar
• ZHANG Y, PROENCA R, MAFFEI M, BARONE M, LEOPOLD L, FRIEDMAN JM: Positional cloning of the mouse obese gene and its human homologue. Nature (1994) 372(6505):425-432.
   PubMed Web of Science ®Google Scholar
• FRIEDMAN JM AND HALAAS JL: Leptin and the regulation of body weight in mammals. Nature (1998) 395(6704):763-770.
   PubMed Web of Science ®Google Scholar
• FLIER JS: Obesity wars: molecular progress confronts an expanding epidemic. Cell (2004) 116(2):337-350.
   PubMed Web of Science ®Google Scholar
• OBICI S, ROSSETTI L: Minireview: nutrient sensing and the regulation of insulin action and energy balance. Endocrinology (2003) 144(12):5172-5178.
   PubMed Web of Science ®Google Scholar
• REN D, LI M, DUAN C, RUI L: Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice. Cell Metab. (2005) 2(2):95-104.
   PubMed Web of Science ®Google Scholar
• FAROOQI I S, JEBB SA, LANGMACK G et al.: Effects of recombinant leptin therapy in a child with congenital leptin deficiency. N. Engl. J. Med. (1999) 341(12):879-884.
   PubMed Web of Science ®Google Scholar
• FAROOQI IS, MATARESE G, LORD GM et al.: Beneficial effects of leptin on obesity, T cell hyporesponsiveness, and neuroendocrine/metabolic dysfunction of human congenital leptin deficiency. J. Clin. Invest. (2002) 110(8):1093-1103.
   PubMed Web of Science ®Google Scholar
• MONTAGUE CT, FAROOQI IS, WHITEHEAD JP et al.: Congenital leptin deficiency is associated with severe early-onset obesity in humans. Nature (1997) 387(6636):903-908.
   PubMed Web of Science ®Google Scholar
• ORAL E A, SIMHA V, RUIZ E et al.: Leptin-replacement therapy for lipodystrophy. N. Engl. J. Med. (2002) 346(8):570-578.
   PubMed Web of Science ®Google Scholar
• HEYMSFIELD SB, GREENBERG AS, FUJIOKA K et al.: Recombinant leptin for weight loss in obese and lean adults: a randomized, controlled, dose-escalation trial. JAMA (1999) 282(16):1568-1575.
   PubMed Web of Science ®Google Scholar
• HALAAS JL, BOOZER C, BLAIR-WEST J, FIDAHUSEIN N, DENTON DA, FRIEDMAN JM: Physiological response to long-term peripheral and central leptin infusion in lean and obese mice. Proc. Natl. Acad. Sci. USA (1997) 94(16):8878-8883.
   PubMed Web of Science ®Google Scholar
• LAI LA, ZHAO C, ZHANG EE, FENG GS: The Shp-2 tyrosine phosphatase. In: Protein phosphatases (Arino J and Alexander D, Eds.), Springer-Verlag, Berlin Heidelberg (2003):275-299.
   Google Scholar
• NEEL BG, GU H, PAO L: The ‘Shp’ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. (2003) 28(6):284-293.
   PubMed Web of Science ®Google Scholar
• PERKINS LA, LARSEN I, PERRIMON N: Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell (1992) 70(2):225-236.
   PubMed Web of Science ®Google Scholar
• HERBST R, CARROLL PM, ALLARD JD, SCHILLING J, RAABE T, SIMON MA: Daughter of sevenless is a substrate of the phosphotyrosine phosphatase Corkscrew and functions during sevenless signaling. Cell (1996) 85(6):899-909.
   PubMed Web of Science ®Google Scholar
• RAABE T, RIESGO-ESCOVAR J, LIU X et al.: DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and Ras1 in Drosophila. Cell (1996) 85(6):911-920.
   PubMed Web of Science ®Google Scholar
• HOF P, PLUSKEY S, DHE-PAGANON S, ECK MJ, SHOELSON SE: Crystal structure of the tyrosine phosphatase SHP-2. Cell (1998) 92(4):441-450.
   PubMed Web of Science ®Google Scholar
• O’REILLY AM, PLUSKEY S, SHOELSON SE, NEEL BG: Activated mutants of SHP-2 preferentially induce elongation of Xenopus animal caps. Mol. Cell. Biol. (2000) 20(1):299-311.
   PubMed Web of Science ®Google Scholar
• CARPENTER LR, FARRUGGELLA TJ, SYMES A, KAROW ML, YANCOPOULOS GD, STAHL N: Enhancing leptin response by preventing SH2-containing phosphatase 2 interaction with Ob receptor. Proc. Natl. Acad. Sci. USA (1998) 95(11):6061-6066.
   PubMed Web of Science ®Google Scholar
• LI C, FRIEDMAN JM: Leptin receptor activation of SH2 domain containing protein tyrosine phosphatase 2 modulates Ob receptor signal transduction. Proc. Natl. Acad. Sci. USA (1999) 96(17):9677-9682.
   PubMed Web of Science ®Google Scholar
• DUAN C, LI M, RUI L: SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated activation of the phosphatidylinositol 3-kinase pathway in response to leptin. J Biol. Chem. (2004) 279(42):43684-43691.
   PubMed Web of Science ®Google Scholar
• BJORBAK C, LAVERY HJ, BATES SH et al.: SOCS3 mediates feedback inhibition of the leptin receptor via Tyr985. J. Biol. Chem. (2000) 275(51):40649-4057.
   PubMed Web of Science ®Google Scholar
• LI W, NISHIMURA R, KASHISHIAN A et al.: A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase. Mol. Cell. Biol. (1994) 14(1):509-517.
   PubMed Web of Science ®Google Scholar
• ARAKI T, NAWA H, NEEL BG: Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors. J. Biol. Chem. (2003) 278(43):41677-41684.
   PubMedGoogle Scholar
• BJORBAEK C, BUCHHOLZ RM, DAVIS SM et al.: Divergent roles of SHP-2 in ERK activation by leptin receptors. J. Biol. Chem. (2001) 276(7):4747-4755.
   PubMedGoogle Scholar
• FENG GS, PAWSON T: Phosphotyrosine phosphatases with SH2 domains: regulators of signal transduction. Trends Genet. (1994) 10(2):54-58.
   PubMed Web of Science ®Google Scholar
• DRAGATSIS I, ZEITLIN S: CaMKIIalpha-Cre transgene expression and recombination patterns in the mouse brain. Genesis (2000) 26(2):133-135.
   PubMed Web of Science ®Google Scholar
• ZHANG EE, CHAPEAU E, HAGIHARA K, FENG GS: Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism. Proc. Natl. Acad. Sci. USA (2004) 101(45):16064-16069.
   PubMedGoogle Scholar
• VAISSE C, HALAAS JL, HORVATH CM, DARNELL JE Jr, STOFFEL M, FRIEDMAN JM: Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice. Nat. Genet. (1996) 14(1):95-97.
   PubMed Web of Science ®Google Scholar
• BATES SH, STEARNS WH, DUNDON TA et al.: STAT3 signalling is required for leptin regulation of energy balance but not reproduction. Nature (2003) 421(6925):856-859.
   PubMed Web of Science ®Google Scholar
• GAO Q, WOLFGANG MJ, NESCHEN S et al.: Disruption of neural signal transducer and activator of transcription 3 causes obesity, diabetes, infertility, and thermal dysregulation. Proc. Natl. Acad. Sci. USA (2004) 101(13):4661-4666.
   PubMed Web of Science ®Google Scholar
• KAMOHARA S, BURCELIN R, HALAAS JL, FRIEDMAN JM, CHARRON MJ: Acute stimulation of glucose metabolism in mice by leptin treatment. Nature (1997) 389(6649):374-377.
   PubMed Web of Science ®Google Scholar
• LEVIN N, LEVIN N, NELSON C, GURNEY A, VANDLEN R, DE SAUVAGE F: Decreased food intake does not completely account for adiposity reduction after ob protein infusion. Proc. Natl. Acad. Sci. USA (1996) 93(4):1726-1730.
   PubMed Web of Science ®Google Scholar
• COHEN P, MIYAZAKI M, SOCCI ND et al.: Role for stearoyl-CoA desaturase-1 in leptin-mediated weight loss. Science (2002) 297(5579):240-243.
   PubMed Web of Science ®Google Scholar
• HALAAS JL, GAJIWALA KS, MAFFEI M et al.: Weight-reducing effects of the plasma protein encoded by the obese gene. Science (1995) 269(5223):543-546.
   PubMed Web of Science ®Google Scholar
• PELLEYMOUNTER, MA, CULLEN MJ, BAKER MB et al.: Effects of the obese gene product on body weight regulation in ob/ob mice. Science (1995) 269(5223):540-543.
   PubMed Web of Science ®Google Scholar
• SHIMOMURA I, HAMMER RE, IKEMOTO S, BROWN MS, GOLDSTEIN JL: Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy. Nature (1999) 401(6748):73-76.
   PubMed Web of Science ®Google Scholar
• KAHN BB, ALQUIER T, CARLING D, HARDIE DG: AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell. Metab. (2005) 1(1):15-25.
   PubMed Web of Science ®Google Scholar
• BRUNING JC, GAUTAM D, BURKS DJ et al.: Role of brain insulin receptor in control of body weight and reproduction. Science (2000) 289(5487):2122-2125.
   PubMed Web of Science ®Google Scholar
• KAZLAUSKAS A, FENG GS, PAWSON T, VALIUS M: The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc. Natl. Acad. Sci. USA (1993) 90(15):6939-6943.
   PubMed Web of Science ®Google Scholar
• LECHLEIDER RJ, SUGIMOTO S, BENNETT AM et al.: Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J. Biol. Chem. (1993) 268(29):21478-21481.
   PubMedGoogle Scholar
• OHTANI T, ISHIHARA K, ATSUMI T et al.: Dissection of signaling cascades through gp130 in vivo: reciprocal roles for STAT3- and SHP2-mediated signals in immune responses. Immunity (2000) 12(1):95-105.
   PubMed Web of Science ®Google Scholar
• SCHMITZ J, WEISSENBACH M, HAAN S, HEINRICH PC, SCHAPER F: SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130. J. Biol. Chem. (2000) 275(17):12848-12856.
   PubMed Web of Science ®Google Scholar
• HIGASHI H, TSUTSUMI R, MUTO S et al.: SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science (2002) 295(5555):683-686.
   PubMed Web of Science ®Google Scholar
• YOU M, YU DH, FENG GS: Shp-2 tyrosine phosphatase functions as a negative regulator in the interferon-stimulated Jak/STAT pathway. Mol. Cell. Biol. (1999) 19:2416-2424.
   PubMed Web of Science ®Google Scholar
• ALI S, CHEN Z, LEBRUN JJ et al.: PTP1D is a positive regulator of the prolactin signal leading to beta-casein promoter activation. EMBO J. (1996) 15(1):135-142.
   PubMed Web of Science ®Google Scholar
• YOU M, FLICK LM, YU D, FENG GS: Modulation of the nuclear factor kappaB pathway by Shp-2 tyrosine phosphatase in mediating the induction of interleukin (IL)-6 by IL-1 or tumor necrosis factor. J. Exp. Med. (2001) 193(1):101-110.
   PubMedGoogle Scholar
• HAKAK Y, HSU YS, MARTIN GS: Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt. Oncogene (2000) 19(28):3164-3171.
   PubMedGoogle Scholar
• WU CJ, O’ROURKE DM, FENG GS, JOHNSON GR, WANG Q, GREENE MI: The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors. Oncogene (2001) 20(42):6018-6025.
   PubMed Web of Science ®Google Scholar
• IVINS ZITO C, KONTARIDIS MI, FORNARO M, FENG GS, BENNETT AM: SHP-2 regulates the phosphatidylinositide 3’-kinase/Akt pathway and suppresses caspase 3-mediated apoptosis. J. Cell. Physiol. (2004) 199(2):227-236.
   PubMed Web of Science ®Google Scholar
• YU DH, QU CK, HENEGARIU O, LU X, FENG GS: Protein tyrosine phosphatase Shp-2 regulates cell spreading, migration and focal adhesion. J. Biol. Chem. (1998) 273:21125-21131.
   PubMed Web of Science ®Google Scholar
• OH ES, GU H, SAXTON TM et al.: Regulation of early events in integrin signaling by protein tyrosine phosphatase SHP-2. Mol. Cell. Biol. (1999) 19(4):3205-3215.
   PubMedGoogle Scholar
• MIAO H, BURNETT E, KINCH M, SIMON E, WANG B: Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. (2000) 2(2):62-69.
   PubMed Web of Science ®Google Scholar
• TONG J, KILLEEN M, STEVEN R, BINNS KL, CULOTTI J, PAWSON T: Netrin stimulates tyrosine phosphorylation of the UNC-5 family of netrin receptors and induces Shp2 binding to the RCM cytodomain. J. Biol. Chem. (2001) 276(44):40917-40925.
   PubMedGoogle Scholar
• TAKAI S, YAMADA M, ARAKI T, KOSHIMIZU H, NAWA H, HATANAKA H: Shp-2 positively regulates brain-derived neurotrophic factor-promoted survival of cultured ventral mesencephalic dopaminergic neurons through a brain immunoglobulin-like molecule with tyrosine-based activation motifs/Shp substrate-1. J. Neurochem. (2002) 82(2):353-3564.
   PubMedGoogle Scholar
• RUSANESCU G, YANG W, BAI A, NEEL BG, FEIG LA: Tyrosine phosphatase SHP-2 is a mediator of activity-dependent neuronal excitotoxicity. EMBO. J. (2005) 24(2):305-314.
   PubMed Web of Science ®Google Scholar
• TARTAGLIA M, MEHLER EL, GOLDBERG R et al.: Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat. Genet. (2001) 29(4):465-468.
   PubMed Web of Science ®Google Scholar
• KEILHACK H, DAVID FS, MCGREGOR M, CANTLEY LC, NEEL BG: Diverse biochemical properties of Shp2 mutants. Implications for disease phenotypes. J. Biol. Chem. (2005) 280(35):30984-30993.
   PubMed Web of Science ®Google Scholar
• ARAKI T, MOHI MG, ISMAT FA et al.: Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation. Nat. Med. (2004) 10(8):849-857.
   PubMed Web of Science ®Google Scholar
• TARTAGLIA M, NIEMEYER CM, FRAGALE A et al.: Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia. Nat. Genet. (2003) 34(2):148-150.
   PubMed Web of Science ®Google Scholar
• YANG J, LIU L, HE D et al.: Crystal structure of human protein-tyrosine phosphatase SHP-1. J. Biol. Chem. (2003) 278(8):6516-6520.
   PubMedGoogle Scholar