PTPN9
Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.[3][4]
Function
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.[4]
References
Further reading
- Kruger JM, Fukushima T, Cherepanov V, et al. (2002). "Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides". J. Biol. Chem. 277 (4): 2620–8. doi:10.1074/jbc.M104550200. PMID 11711529.
- Qi Y, Zhao R, Cao H, et al. (2002). "Purification and characterization of protein tyrosine phosphatase PTP-MEG2". J. Cell. Biochem. 86 (1): 79–89. doi:10.1002/jcb.10195. PMID 12112018.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241
. PMID 12477932.
- Pasquali C, Curchod ML, Wälchli S, et al. (2004). "Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor". Mol. Endocrinol. 17 (11): 2228–39. doi:10.1210/me.2003-0011. PMID 12907755.
- 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". Blood. 102 (13): 4354–60. doi:10.1182/blood-2003-04-1308. PMID 12920026.
- 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. PMID 14662869.
- 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. PMID 15322554.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- 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. PMID 16679294.
- 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. PMID 17387180.
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| 2pa5: Crystal structure of human protein tyrosine phosphatase PTPN9 |
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