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Review
. 2020 Dec 11;10(12):1659.
doi: 10.3390/biom10121659.

Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer

Affiliations
Review

Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer

Soha Mcheik et al. Biomolecules. .

Abstract

In this review article, we present the current knowledge on PTPN13, a class I non-receptor protein tyrosine phosphatase identified in 1994. We focus particularly on its role in cancer, where PTPN13 acts as an oncogenic protein and also a tumor suppressor. To try to understand these apparent contradictory functions, we discuss PTPN13 implication in the FAS and oncogenic tyrosine kinase signaling pathways and in the associated biological activities, as well as its post-transcriptional and epigenetic regulation. Then, we describe PTPN13 clinical significance as a prognostic marker in different cancer types and its impact on anti-cancer treatment sensitivity. Finally, we present future research axes following recent findings on its role in cell junction regulation that implicate PTPN13 in cell death and cell migration, two major hallmarks of tumor formation and progression.

Keywords: PTPN13; cancer; cell signaling; oncogene; tumor suppressor.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
PTPN13 structure, interactions, and substrates. Interactors or substrates in green were involved in PTPN13 tumor suppressor role. Interactors or substrates in red were involved in PTPN13 pro-tumoral role. KIND domain: kinase non-catalytic C-lobe domain (unknow function), FERM: 4.1/Ezrin/radixin/moesin domain (protein/protein and protein/plasma membrane interaction), PDZ domains: PSD95/Dlg1/Zo-1 domain (protein/protein interaction domain), Calp2: Calpain-2, β-cat: β-catenin.
Figure 2
Figure 2
PTPN13 is involved in multiple signaling pathways. PTPN13 in green: Tumor suppressor role; PTPN13 in red: Pro-tumoral role. Arrow pointing to P: PTPN13 effects mediated by its phosphatase activity. TLR: Toll-like receptor, LRP/Fz: lipoprotein receptor-related protein/Frizzled.

References

    1. Maekawa K., Imagawa N., Nagamatsu M., Harada S. Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats. FEBS Lett. 1994;337:200–206. doi: 10.1016/0014-5793(94)80273-4. - DOI - PubMed
    1. Banville D., Ahmad S., Stocco R., Shen S.H. A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J. Biol. Chem. 1994;269:22320–22327. - PubMed
    1. Saras J., Claesson-Welsh L., Heldin C.H., Gonez L.J. Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. J. Biol. Chem. 1994;269:24082–24089. - PubMed
    1. Sato T., Irie S., Kitada S., Reed J.C. FAP-1: A protein tyrosine phosphatase that associates with Fas. Science. 1995;268:411–415. doi: 10.1126/science.7536343. - DOI - PubMed
    1. Julien S.G., Dubé N., Hardy S., Tremblay M.L. Inside the human cancer tyrosine phosphatome. Nat. Rev. Cancer. 2011;11:35–49. doi: 10.1038/nrc2980. - DOI - PubMed

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