Protein tyrosine phosphatase Meg2 dephosphorylates signal transducer and activator of transcription 3 and suppresses tumor growth in breast cancer

@article{Su2011ProteinTP,
  title={Protein tyrosine phosphatase Meg2 dephosphorylates signal transducer and activator of transcription 3 and suppresses tumor growth in breast cancer},
  author={Fuqin Su and F. Ren and Yu Rong and Yangmeng Wang and Yongtao Geng and Yinyin Wang and Mengyao Feng and Yanfang Ju and Y. Li and Z. Zhao and K. Meng and Z. Chang},
  journal={Breast Cancer Research : BCR},
  year={2011},
  volume={14},
  pages={R38 - R38}
}
IntroductionSignal transducer and activator of transcription 3 (STAT3) is over-activated or phosphorylated in breast cancers. The hyper-phosphorylation of STAT3 was attributed to either up-regulated phosphorylation by several tyrosine-kinases or down-regulated activity of phosphatases. Although several factors have been identified to phosphorylate STAT3, it remains unclear how STAT3 is dephosphorylated by PTPMeg2. The aim of this study was to determine the role of PTPMeg2 as a phosphatase in… Expand
Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling
TLDR
There are seven PTPs that have been shown to dephosphorylate STAT3 and, thereby, regulate STAT3 signaling and have great potential as targets for the development of more effective therapies against human disease, including cancer. Expand
Sugiol inhibits STAT3 activity via regulation of transketolase and ROS-mediated ERK activation in DU145 prostate carcinoma cells.
TLDR
Sugiol is the first compound regulating STAT3 activity via modulation of cancer metabolic pathway and the use of sugiol as an inhibitor of the STAT3 pathway for the treatment of human solid tumors with activated STAT3 is suggested. Expand
PTPN9 promotes cell proliferation and invasion in Eca109 cells and is negatively regulated by microRNA-126
TLDR
This is the first study to demonstrate that PTPN9 is overexpressed in ESCC and associated with poor survival, and may therefore be important in the pathogenesis of ESCC. Expand
PTPN9 induces cell apoptosis by mitigating the activation of Stat3 and acts as a tumor suppressor in colorectal cancer
TLDR
It is indicated that PTPN9 inhibits cell growth and survival by repressing the activation of Stat3 in colorectal cancer, which suggests an important underlying mechanism of regulating cell Growth and provides a novel candidate therapeutic target for coloreCTal cancer. Expand
β-Arrestin 1’s Interaction with TC45 Attenuates Stat signaling by dephosphorylating Stat to inhibit antimicrobial peptide expression
TLDR
It is reported that β-arrestin1 interacts with TC45 (45-kDa form of T cell protein tyrosine phosphatase) in the nucleus to attenuate Stat signaling by promoting dephosphorylation of Stat. Expand
GdX/UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis.
TLDR
GdX (UBL4A) promotes STAT3 dephosphorylation via mediating the interaction between TC45 (the nuclear isoform of TC-PTP) and STAT3 specifically and stabilizes the TC45-STAT3 complex to bestow upon STAT3 an efficient deph phosphorylation by TC45. Expand
MEG2 is regulated by miR-181a-5p and functions as a tumour suppressor gene to suppress the proliferation and migration of gastric cancer cells
TLDR
It is found that MEG2 is downregulated in human gastric cancer and that miR-181a-5p is predicted to be a potential regulator of M EG2. Expand
The Opposing Function of STAT3 as an Oncoprotein and Tumor Suppressor Is Dictated by the Expression Status of STAT3β in Esophageal Squamous Cell Carcinoma
TLDR
STAT3β suppresses chemoresistance and cancer stemness by blocking the transcriptional activity of STAT3α, one of the two STAT3 isoforms, and is an independent protective prognostic marker in patients with ESCC. Expand
Protein tyrosine phosphatase PTPN9 regulates erythroid cell development through STAT3 dephosphorylation in zebrafish
TLDR
Findings imply that PTPN9 plays an important role in erythropoiesis by disrupting an inhibitory complex of phosphorylated STAT3, GATA1 and ZBP-89, providing new cellular and molecular insights into the role of ptpn9a in developmental hematopoiesi. Expand
STAT3 inhibitors: finding a home in lymphoma and leukemia.
TLDR
Targeting the STAT pathway, which seems to be critical in tumorigenesis, is promising for multiple malignancies including lymphoma and leukemia, and mechanisms of action, failures, and successes of STAT3 inhibitors are reviewed. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 43 REFERENCES
PTP1B suppresses prolactin activation of Stat5 in breast cancer cells.
TLDR
The data implicate PTP1B as an important negative regulator of Stat5 phosphorylation in invasive breast cancer. Expand
Identification of a Nuclear Stat1 Protein Tyrosine Phosphatase
TLDR
The results identify TC45 as a PTP responsible for the dephosphorylation of Stat1 in the nucleus, the nuclear isoform of the T-cell PTP (TC-PTP). Expand
The putative tumor suppressor gene PTPN13/PTPL1 induces apoptosis through insulin receptor substrate-1 dephosphorylation.
TLDR
Data provide the first evidence for a direct positive role of the putative tumor suppressor gene PTPL1/PTPN13 on apoptosis and identify its target in the IRS-1/PI3K/Akt signaling pathway. Expand
A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus.
TLDR
Taken together, these observations conclude that TC-PTP is catalytically competent with respect to dephosphorylation and deactivation of PRL-activated STAT5 in the nucleus. Expand
PTP1B is a negative regulator of interleukin 4-induced STAT6 signaling.
TLDR
It is shown that PTP1B expression may be preferentially elevated in activated B cell-like diffuse large B-cell lymphomas and a novel regulatory loop for the regulation of IL-4-induced STAT6 signaling is delineated that may have important implications in both neoplastic and inflammatory processes. Expand
Prolactin Induces SHP-2 Association with Stat5, Nuclear Translocation, and Binding to the β-Casein Gene Promoter in Mammary Cells*
TLDR
A tight physical and functional interaction between SHP2 and Stat5 required for regulation and perpetuation of PRL-mediated signaling in mammary cells is indicated and a potential role for SHP-2 in the nucleus is suggested. Expand
Protein-tyrosine Phosphatase PTPN9 Negatively Regulates ErbB2 and Epidermal Growth Factor Receptor Signaling in Breast Cancer Cells*
TLDR
PTPN9 is suggested as a negative regulator of breast cancer cells by targeting ErbB2 and EGFR and inhibiting STAT activation and reducing invasion and MMP2 expression of MDA-MB-231 cells. Expand
PTP 1 B is a negative regulator of interleukin 4 – induced STAT 6 signaling
Protein tyrosine phosphatase 1B (PTP1B) is a ubiquitously expressed enzyme shown to negatively regulate multiple tyrosine phosphorylation-dependent signaling pathways. PTP1B can modulate cytokineExpand
New and Old Functions of STAT3: A Pivitol Target for Individualized Treatment of Cancer
TLDR
Genetic tools to evaluate STAT-dependent malignancy are developed and it is shown that survival and growth of lymphoid malignancies requires expression of STAT3 and STAT3-null fibroblasts are resistant to transformation by a variety of oncogenes. Expand
PTPL1/PTPN13 regulates breast cancer cell aggressiveness through direct inactivation of Src kinase.
TLDR
PTPL1 is identified as the first phosphatase able to inhibit Src through direct dephosphorylation in intact cells, and a new mechanism by which PTPL1 inhibits breast tumor aggressiveness is described. Expand
...
1
2
3
4
5
...