Difference between revisions of "Phosphatase Subfamily PTPN9"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:[[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN9|Subfamily PTPN9]] (MEG2/PTPMEG2) | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:[[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN9|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=== | ===Evolution=== | ||
| − | + | PTPN9 emerged in metazoan, usually one copy per genome. | |
===Domain === | ===Domain === | ||
| − | PTPN9 has two domains: a N-terminal domain homologous to yeast | + | PTPN9 has two domains: a N-terminal domain homologous to yeast Sec14p and a C-terminal phosphatase domain <cite>Gu92</cite>. |
| + | |||
| + | 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 <cite>Huynh03</cite> and/or mannose 6-phosphate receptor-interacting protein TIP47 and Arfaptin2 on vesicles <cite>Saito07</cite>. | ||
===Functions=== | ===Functions=== | ||
PTPN9 is widely expressed in different tissues <cite>Gu92</cite> (also see [http://www.gtexportal.org/home/gene/PTPN9 GTEx]). | PTPN9 is widely expressed in different tissues <cite>Gu92</cite> (also see [http://www.gtexportal.org/home/gene/PTPN9 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 <cite>Huynh03</cite> and/or mannose 6-phosphate receptor-interacting protein TIP47 and Arfaptin2 on vesicles <cite>Saito07</cite>. 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 <cite>Huynh04</cite>. | ||
| + | |||
| + | 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 <cite>Kruger02</cite>. | ||
| + | |||
| + | PTPN9/PTPMEG2 directly interacts with STAT3 and mediates its dephosphorylation in the cytoplasm <cite>Su12</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 also has an important role in the development of erythroid cells <cite>Xu03</cite>. | ||
===References=== | ===References=== | ||
<biblio> | <biblio> | ||
#Gu92 pmid=1557404 | #Gu92 pmid=1557404 | ||
| + | #Hao12 pmid=22763125 | ||
| + | #Huynh03 pmid=14662869 | ||
| + | #Huynh04 pmid=15322554 | ||
| + | #Kruger02 pmid=11711529 | ||
| + | #Saito07 pmid=17387180 | ||
| + | #Su12 pmid=22394684 | ||
| + | #Xu03 pmid=12920026 | ||
| + | #Yuan10 pmid=20335174 | ||
</biblio> | </biblio> | ||
Revision as of 00:16, 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 also has an important role in the development of erythroid cells [9].
References
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- Error fetching PMID 14662869:
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