| Cible |
EC:3.1.3.86, INPPL-1, INPPL1, Inositol polyphosphate phosphatase-like protein 1, Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2, Protein 51C, SH2 domain-containing inositol 5'-phosphatase 2, SH2 domain-containing inositol phosphatase 2, SHIP-2, SHIP2 |
| Contexte | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (INPPL1) is a ~138 kDa protein. Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. 1. Vandeput, F. et al. (2006) Cellular signalling 18, 2193-9. PMID: 168247322. Habib, T. et al. (1998) The Journal of biological chemistry 273, 18605-9. PMID: 96608333. Dyson, JM. et al. (2001) The Journal of cell biology 155, 1065-79. PMID: 117394145. Prasad, NK. et al. (2005) The Journal of biological chemistry 280, 13129-36. PMID: 156682406. Hasegawa, J. et al. (2011) The Journal of cell biology 193, 901-16. PMID: 216249567. Prasad, N. et al. (2002) Journal of cell science 115, 3807-15. PMID: 122352919. Zhuang, G. et al. (2007) The Journal of biological chemistry 282, 2683-94. PMID: 1713524010. Pengal, RA. et al. (2003) The Journal of biological chemistry 278, 22657-63. PMID: 12690104 |
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