The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by poly-phosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.
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Xu MJ, Sui X, Zhao R, et al. (2004). "PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells". Blood102 (13): 4354–60. doi:10.1182/blood-2003-04-1308. PMID12920026.
Huynh H, Wang X, Li W, et al. (2004). "Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells". J. Immunol.171 (12): 6661–71. doi:10.4049/jimmunol.171.12.6661. PMID14662869.
Huynh H, Bottini N, Williams S, et al. (2004). "Control of vesicle fusion by a tyrosine phosphatase". Nat. Cell Biol.6 (9): 831–9. doi:10.1038/ncb1164. PMID15322554.
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Cho CY, Koo SH, Wang Y, et al. (2007). "Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling". Cell Metab.3 (5): 367–78. doi:10.1016/j.cmet.2006.03.006. PMID16679294.
Saito K, Williams S, Bulankina A, et al. (2007). "Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins". J. Biol. Chem.282 (20): 15170–8. doi:10.1074/jbc.M608682200. PMID17387180.