Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity

Nature Medicine

Volumn 11, Issue 2, 2005, Pages 199-205

  Sleeman, Mark W ^a   Wortley, Katherine E ^a   Lai, Ka Man V ^a   Gowen, Lori C ^a   Kintner, Jennifer ^a   Kline, William O ^a   Garcia, Karen ^a   Stitt, Trevor N ^a   Yancopoulos, George D ^a   Wiegand, Stanley J ^a   Glass, David J ^a  

^a REGENERON PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DIET; EXON; FEMALE; GENE; GENE DELETION; GENETIC CODE; GLUCOSE HOMEOSTASIS; GLUCOSE TOLERANCE; INPPL1 GENE; INSULIN SENSITIVITY; INSULIN TOLERANCE TEST; LIPID DIET; MALE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OBESITY; PERINATAL DEATH; PHOX2A GENE; PRIORITY JOURNAL; SHIP2 GENE; TRANSLATION INITIATION; WEIGHT GAIN;

ANIMALS; BLOOD CHEMICAL ANALYSIS; BODY WEIGHT; DIETARY FATS; EXONS; FEMALE; GENE DELETION; GENES, REPORTER; GLUCOSE; HOMEOSTASIS; INSULIN; MALE; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; OBESITY; PHENOTYPE; PHOSPHORIC MONOESTER HYDROLASES; SIGNAL TRANSDUCTION; TISSUE DISTRIBUTION;

EID: 20044364159     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm1178     Document Type: Article

References (40)

1. 125I]-insulin binding plasma membrane fraction from rat liver. Biochem. Biophys. Res. Commun. 41, 541-548 (1970).
2. 125I)insulin to the plasma membrane and its relation to insulin bioactivity. Proc. Natl. Acad. Sci. USA 68, 1833-1837 (1971).
3. Cuatrecasas, P. Properties of the insulin receptor of isolated fat cell membranes. J. Biol. Chem. 246, 7265-7274 (1971).
4. Kasuga, M., Karlsson, F.A. & Kahn, C.R. Insulin stimulates the phosphorylation of the 95,000-Dalton subunit of its own receptor. Science 215, 185-187 (1982).
5. Asante-Appiah, E. & Kennedy, B.P. Protein tyrosine phosphatases: the quest for negative regulators of insulin action. Am. J. Physiol. Endocrinol. Metab. 284, E663-E670 (2003).
6. Elchebly, M. et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1b gene. Science 283, 1544-1548 (1999).
7. Klaman, L.D. et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1b-deficient mice. Mol. Cell. Biol. 20, 5479-5489 (2000).
8. Sun, X.J. et al. Structure of the insulin receptor substrate IRS-1 definesa unique signal transduction protein. Nature 352, 73-77 (1991).
9. Hadari, Y.R. et al. Insulin and insulinomimetic agents induce activation of phosphatidylinositol 3-kinase upon its association with pp185 (IRS-1) in intact rat livers. J. Biol. Chem. 267, 17483-17486 (1992).
10. Burgering, B.M. & Coffer, P.J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376, 599-602 (1995).
11. Franke, T.F. et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736 (1995).
12. Whitman, M., Downes, C.P., Keeler, M., Keller, T. & Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332, 644-646 (1988).
13. Toker, A. & Cantley, L.C. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387, 673-676 (1997).
14. Alessi, D.R. et al. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha. Curr. Biol. 7, 261-269 (1997).
15. Andielkovic, M. et al. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524 (1997).
16. Andjelkovic, M. et al. Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors. Proc. Natl. Acad. Sci. USA 93, 5699-5704 (1996).
17. Chen, W.S. et al. Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene. Genes Dev. 15, 2203-2208 (2001).
18. Cho, H. et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 292, 1728-1731. (2001).
19. Katome, T. et al. Use of RNA-interference-mediated gene silencing and adenoviral overexpression to elucidate the roles of AKT/PKB-isoforms in insulin actions. J. Biol. Chem. 278, 28312-28323 (2003).
20. Summers, S.A., Garza, L.A., Zhou, H. & Birnbaum, M.J. Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Mol. Cell. Biol. 18, 5457-5464 (1998).
21. Hill, M.M. et al. A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes. Mol. Cell. Biol. 19, 7771-7781 (1999).
22. Sakoda, G. et al. Differing roles of Akt and serum- and glucocorticoid-regulated kinase in glucose metabolism, DNA synthesis, and oncogenic activity. J. Biol. Chem. 278, 25802-25807 (2003).
23. Brunet, A. et al. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21, 952-965 (2001).
24. Hertweck, M., Gobel, C. & Baumeister, R. C. elegans SGK-1 is the critical component in the Akt/PKB kinase complex to control stress response and life span. Dev. Cell 6, 577-588 (2004).
25. Damen, J.E. et al. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93, 1689-1693 (1996).
26. Stambolic, V. et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95, 29-39. (1998).
27. Liu, L. et al. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis. J. Biol. Chem. 272, 8983-8988 (1997).
28. Lamkin, T.D. et al. Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J. Biol. Chem. 272, 10396-401 (1997).
29. Pesesse, X., Deleu, S., De Smedt, F., Drayer, L. & Erneux, C. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem. Biophys. Res. Commun. 239, 697-700 (1997).
30. Pesesse, X. et al. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. FEBS Lett. 437, 301-303 (1998).
31. Aman, M.J., Lamkin, T.D., Okada, H., Kurosaki, T. & Ravichandran, K.S. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J. Biol. Chem. 273, 33922-33928 (1998).
32. Clement, S. et al. The lipid phosphatase SHIP2 controls insulin sensitivity. Nature 409, 92-97 (2001).
33. Wada, T. et al. Overexpression of SH2-Containing Inositol Phosphatase 2 Results in Negative Regulation of Insulin-Induced Metabolic Actions in 3T3-L1 Adipocytes via Its 5-Phosphatase Catalytic Activity. Mol. Cell. Biol. 21, 1633-1646 (2001).
34. Alessi, D.R. et al. 3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homologywith the Drosophila DSTPK61 kinase. Curr. Biol. 7, 776-789 (1997).
35. Rommel, C. et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat. Cell Biol. 3, 1009-1013 (2001).
36. Bodine, S.C. et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3, 1014-1019 (2001).
37. Boss, O. et al. Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression. FEBS Lett. 408, 39-42 (1997).
38. Clement, S. et al. Corrigendum: The lipid phosphatase SHIP2 controls insulin sensitivity. Nature 431, 878 (2004).
39. Valenzuela, D. et al. High-throughput engineering of the mouse genome coupled with high-resolution expression analysis. Nat. Biotechnol. 21, 652-659 (2003).
40. Sleeman, M.W. et al. Ciliary neurotrophic factor improves diabetic parameters and hepatic steatosis and increases basal metabolic rate in db/db mice. Proc. Natl. Acad. Sci. USA 100, 14297-14302 (2003).