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Int. J. Mol. Sci. 2018, 19(9), 2708; https://doi.org/10.3390/ijms19092708

Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling

1
Department of Biomedical Sciences, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA
2
Department of Human Genetics, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA
3
South Texas Diabetes and Obesity Institute, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA
4
Division of Bioconvergence Analysis, Korea Basic Science Institute, Daejeon 305-333, Korea
5
Integrated Research Institute of Pharmaceutical Science & BK21 PLUS Team for Creative Leader Program for Pharmacomics-based Future Pharmacy, College of Pharmacy, The Catholic University of Korea, Bucheon-si, Gyeonggi-do 420-743, Korea
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 3 August 2018 / Revised: 29 August 2018 / Accepted: 6 September 2018 / Published: 11 September 2018
(This article belongs to the Special Issue Advances in Biological Functions of STAT3)
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Abstract

The signal transducer and activator of transcription 3 (STAT3) protein is a major transcription factor involved in many cellular processes, such as cell growth and proliferation, differentiation, migration, and cell death or cell apoptosis. It is activated in response to a variety of extracellular stimuli including cytokines and growth factors. The aberrant activation of STAT3 contributes to several human diseases, particularly cancer. Consequently, STAT3-mediated signaling continues to be extensively studied in order to identify potential targets for the development of new and more effective clinical therapeutics. STAT3 activation can be regulated, either positively or negatively, by different posttranslational mechanisms including serine or tyrosine phosphorylation/dephosphorylation, acetylation, or demethylation. One of the major mechanisms that negatively regulates STAT3 activation is dephosphorylation of the tyrosine residue essential for its activation by protein tyrosine phosphatases (PTPs). There are seven PTPs that have been shown to dephosphorylate STAT3 and, thereby, regulate STAT3 signaling: PTP receptor-type D (PTPRD), PTP receptor-type T (PTPRT), PTP receptor-type K (PTPRK), Src homology region 2 (SH-2) domain-containing phosphatase 1(SHP1), SH-2 domain-containing phosphatase 2 (SHP2), MEG2/PTP non-receptor type 9 (PTPN9), and T-cell PTP (TC-PTP)/PTP non-receptor type 2 (PTPN2). These regulators have great potential as targets for the development of more effective therapies against human disease, including cancer. View Full-Text
Keywords: STAT3; PTPRT; PTPRD; SHP1; SHP2; TC-PTP STAT3; PTPRT; PTPRD; SHP1; SHP2; TC-PTP
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Kim, M.; Morales, L.D.; Jang, I.-S.; Cho, Y.-Y.; Kim, D.J. Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling. Int. J. Mol. Sci. 2018, 19, 2708.

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