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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Protein tyrosine phosphatase, non-receptor type 9

MEG2, protein tyrosine phosphatase MEG2, PTPN9
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 polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Pts, NS1, TCPTP, Protein-Tyrosine-Phosphatase, SHP1
Papers on MEG2
Downregulated Expression of PTPN9 Contributes to Human Hepatocellular Carcinoma Growth and Progression.
Zhang et al., Nantong, China. In Pathol Oncol Res, Jan 2016
PTPN9 has recently been reported to play a critical role in breast cancer development.
Genetic association of marbling score with intragenic nucleotide variants at selection signals of the bovine genome.
Lee et al., Seoul, South Korea. In Animal, Jan 2016
Genetic associations of MS were found (P<3.88×10-4) with six intragenic nucleotide variants on bovine autosomes 3 (cache domain containing 1, CACHD1), 5 (like-glycosyltransferase, LARGE), 16 (cell division cycle 42 binding protein kinase alpha, CDC42BPA) and 21 (snurportin 1, SNUPN; protein tyrosine phosphatase, non-receptor type 9, PTPN9; chondroitin sulfate proteoglycan 4, CSPG4).
The Opposing Function of STAT3 as an Oncoprotein and Tumor Suppressor Is Dictated by the Expression Status of STAT3β in Esophageal Squamous Cell Carcinoma.
Lai et al., Shantou, China. In Clin Cancer Res, Oct 2015
However, the heterodimer formation decreased the binding between STAT3α and PTPN9 (better known as PTP-MEG2), a protein tyrosine phosphatase, thereby promoting the phosphorylation of STAT3α(Y705) and enhancing its nuclear translocation and DNA binding.
EGFR blockade prevents glioma escape from BRAFV600E targeted therapy.
Nicolaides et al., San Francisco, United States. In Oncotarget, Oct 2015
BRAF(V600E) inhibition suppresses MAPK signaling, which in turn downregulates the EGFR phosphatase PTPN9, resulting in sustained EGFR phosphorylation and enhanced EGFR activity.
Sugiol inhibits STAT3 activity via regulation of transketolase and ROS-mediated ERK activation in DU145 prostate carcinoma cells.
Kwon et al., Taejŏn, South Korea. In Biochem Pharmacol, Oct 2015
The protein phosphatase MEG2 was also responsible for sugiol-induced STAT3 dephosphorylation.
In silico design of a DNA-based HIV-1 multi-epitope vaccine for Chinese populations.
Zhou et al., Beijing, China. In Hum Vaccin Immunother, 2014
We performed an in silico design of 3 DNA vaccines, designated pJW4303-MEG1, pJW4303-MEG2 and pJW4303-MEG3, encoding multi-epitopes that are highly conserved within the HIV-1 subtypes most prevalent in China and can be recognized through HLA alleles dominant in China.
A novel oxybis cresol verticilatin with highly varying degrees of biological activities from the insect pathogenic fungus Paecilomyces verticillatus.
Shi et al., Baoding, China. In J Asian Nat Prod Res, 2014
Fortunately, compound 1 exhibited significant inhibitory activities against CDC25B, cathepsin B, MEG2, and SHP2 enzyme, with IC50 values of 11.5, 3.5, 7.8, and 15 μg/ml, respectively.
A novel C₂₅ sterol peroxide from the endophytic fungus Phoma sp. EA-122.
Liu et al., In Z Naturforsch C, 2014
Phomasterol A (1) was evaluated for its inhibitory activities against protein-tyrosine phosphatases MEG2 and PTP1Bc, showing moderate activities with identical IC₅₀ values of 25 μM.
Proteomics at the schistosome-mammalian host interface: any prospects for diagnostics or vaccines?
Wilson, York, United Kingdom. In Parasitology, 2012
The egg secretions that aid escape from the tissues include a mixture of MEG-2 and MEG-3 family variant proteins.
Signal transducer and activator of transcription 5 as a key signaling pathway in normal mammary gland developmental biology and breast cancer.
Cabrera et al., Washington, D.C., United States. In Breast Cancer Res, 2010
TGF-β and PTPN9 can downregulate prolactin- and EGF-mediated STAT5 activation, respectively.
Protein-tyrosine phosphatase PTPN9 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells.
Gu et al., Denver, United States. In J Biol Chem, 2010
data suggest PTPN9 as a negative regulator of breast cancer cells by targeting ErbB2 and EGFR and inhibiting STAT activation
[Research progress of several protein tyrosine phosphatases in diabetes].
Yu et al., Jinan, China. In Sheng Li Xue Bao, 2010
Several protein tyrosine phosphatases, such as PTP1B (PTPN1), TCPTP (PTPN2), LYP (PTPN22), PTPIA-2, PTPMEG2 (PTPN9) or OSTPTP are involved in insulin signaling pathway, insulin secretion and autoreactive attack to pancreatic beta cells.
Control of granule exocytosis in neutrophils.
Eitzen et al., Edmonton, Canada. In Front Biosci, 2007
Recent observations indicate that receptor-mediated granule release from neutrophils depends on activation of distal signaling pathways that include the src family of tyrosine kinases, beta-arrestins, the tyrosine phosphatase MEG2, the kinase MARCK, Rabs and SNAREs, and the Rho GTPase, Rac2.
Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins.
Mustelin et al., Los Angeles, United States. In J Biol Chem, 2007
the N terminus of PTPMEG2 is necessary for the targeting of this phosphatase to the secretory vesicle compartment by association with other proteins involved in intracellular transport.
Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling.
Chanda et al., San Diego, United States. In Cell Metab, 2006
role in the negative regulation of hepatic insulin signaling
Control of vesicle fusion by a tyrosine phosphatase.
Mustelin et al., Los Angeles, United States. In Nat Cell Biol, 2004
PTP-MEG2 reduced the phosphotyrosine content of NSF and co-localized with NSF and syntaxin 6 in intact cells, the first demonstrated role for a protein tyrosine phosphatase in the regulated secretory pathway
Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells.
Mustelin et al., Los Angeles, United States. In J Immunol, 2004
PTPase-MEG2 through its Sec14p homology domain couples inositide phosphorylation to tyrosine dephosphorylation and the regulation of intracellular traffic of the secretory pathway in T cells.
Nonreceptor protein tyrosine and lipid phosphatases in type I fc(epsilon) receptor-mediated activation of mast cells and basophils.
Dráber et al., Praha, Czech Republic. In Int Arch Allergy Immunol, 2002
This review summarizes the current understanding of the structural and functional aspects of nonreceptor protein tyrosine phosphatases (SHP-1, SHP-2, HePTP, PTP20, PRL1, PRL2, PTP-MEG1 and PTP-MEG2) and lipid phosphatases (SHIP and SHIP2) in the activation of mast cells and basophils after Fc(epsilon)RI aggregation.
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