PTPN9: Human protein tyrosine phosphatase, non-receptor type 9
PDB Code: 2PA5
PTPN9 also called MEG2 was originally cloned from a megakaryocytic cell line and is the only member of the NT3 subfamily of PTPs. This tyrosine phosphatase contains a unique 250-amino-acid non-catalytic N-terminus with homology to Sec14p, a yeast protein that has been described to bind to and is activated by polyphosphoinositides PIP2 and PIP3 as well as by phosphatidyl serine. Deletion of PTPN9 in mice results in multiple neurodevelopmental defects and hemorrhages and a more than 90% late embryonic lethality. PTPN9 has been shown to inhibit insulin-induced phosphorylation of the insulin receptor and subsequent studies showed that RNAi-mediated reduction of PTPN9 transcript levels enhances insulin action. In addition, PTPN9 has been identified as a modulator of the insulin-dependent gluconeogenic transcription factor FOXO1. Importantly, adenoviral-mediated depletion of PTPN9 in the liver of diabetic mice results in insulin sensitization and normalization of hyperglycemia suggesting that modulation of PTPN9 activity may be an effective strategy in the treatment of type 2 diabetes.
PTPN9 has also been implicated in the development of Polycythemia vera (PV), a clonal myeloproliferative disorder characterized by trilineage marrow hyperplasia with increased production of red cells, granulocytes, and platelets. Polycythemia has been associated with high mortality rates if untreated as well as with the development of leukemia. A correlation of PTPN9 activity with colony-forming ability of ECFCs ( erythroid colony-forming cells) has been demonstrated suggesting also PTPN9 as a potential target for development of therapeutic drugs to reduce red cell production.
Here we determined the structure of the phosphatase domain at 1.6 Å resolution.
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