Difference between revisions of "Phosphatase Subfamily PTPN9"
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PTPN9/PTPMEG2 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells <cite>Yuan10</cite>, and vascular endothelial growth factor receptor (perhaps on Tyr-1175) in endothelial cells <cite>Hao12</cite>. | PTPN9/PTPMEG2 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells <cite>Yuan10</cite>, and vascular endothelial growth factor receptor (perhaps on Tyr-1175) in endothelial cells <cite>Hao12</cite>. | ||
| − | PTPN9/PTPMEG2 | + | PTPN9/PTPMEG2 has an important role in the development of erythroid cells <cite>Xu03</cite>. |
| + | |||
| + | The human gene is implicated in signaling between insulin receptor (InsR) and the FoxO transcription factor <cite>Cho06</cite>. | ||
===References=== | ===References=== | ||
Revision as of 00:17, 18 March 2015
Phosphatase Classification: Fold CC1:Superfamily CC1: Family PTP: Subfamily PTPN9 (MEG2/PTPMEG2)
PTPN9/MEG2 is a metazoan subfamily functions in regulated secretory pathway. It has a characteristic accessory domain, a N-terminal Sec14p homology domain, which localizes it to secretory vesicles.
Evolution
PTPN9 emerged in metazoan, usually one copy per genome.
Domain
PTPN9 has two domains: a N-terminal domain homologous to yeast Sec14p and a C-terminal phosphatase domain [1].
The N-terminal Sec14p homology domain localizes the protein to secretory vesicles, by binding to phosphatidylinositol-3,4,5-trisphosphate (PI(3,4,5)P(3)) on secretory vesicle membranes [2] and/or mannose 6-phosphate receptor-interacting protein TIP47 and Arfaptin2 on vesicles [3].
Functions
PTPN9 is widely expressed in different tissues [1] (also see GTEx).
PTPN9/PTPMEG2 plays important role in regulated secretory pathway. It induces homotypic secretory vesicle fusion in cells. PTPN9/PTPMEG2 localizes to secretory vesicle membranes through its N-terminal Sec14p homolog domain binding to phosphatidylinositol-3,4,5-trisphosphate [2] and/or mannose 6-phosphate receptor-interacting protein TIP47 and Arfaptin2 on vesicles [3]. It dephosphorylates N-ethylmaleimide-sensitive factor (NSF), a key regulator of vesicle fusion, at Tyr 83, which resulted in the local release of NSF from a tyrosine-phosphorylated, inactive state [4].
PTPN9/PTPMEG2 localizes to secondary and tertiary granules and secretory vesicles in neutrophils, and may regulate phagocytosis, an essential antimicrobial function in the innate immune response [5].
PTPN9/PTPMEG2 directly interacts with STAT3 and mediates its dephosphorylation in the cytoplasm [6].
PTPN9/PTPMEG2 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells [7], and vascular endothelial growth factor receptor (perhaps on Tyr-1175) in endothelial cells [8].
PTPN9/PTPMEG2 has an important role in the development of erythroid cells [9].
The human gene is implicated in signaling between insulin receptor (InsR) and the FoxO transcription factor [10].
References
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