Historical Background
Phosphorylation of tyrosine residues in proteins is one of the better-studied molecular mechanisms for regulating protein structure and function and with it – the function of cells and organisms. Tyrosine phosphorylation is a reversible process that is controlled by the opposing activities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). The numbers of PTKs and PTPs are similar and small relative to the numbers of their potential substrates; there are 81 and 85 genes that yield active, protein-specific PTPs and PTKs, respectively (Alonso et al. 2004). As a result, individual PTPs and PTKs each target multiple substrates and fulfill distinct roles in different physiological systems. Although PTPs were first described in molecular terms in 1988, about a decade after PTKs, both protein superfamilies are now recognized as critical regulators of protein phosphorylation and...
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References
Aga-Mizrachi S, Brutman-Barazani T, Jacob AI, Bak A, Elson A, Sampson SR. Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle. Endocrinology. 2008;149(2):605–14.
Akimoto M, Mishra K, Lim KT, Tani N, Hisanaga SI, Katagiri T, et al. Protein tyrosine phosphatase epsilon is a negative regulator of FcepsilonRI-mediated mast cell responses. Scand J Immunol. 2009;69(5):401–11.
Alonso A, Sasin J, Bottini N, Friedberg I, Osterman A, Godzik A, et al. Protein tyrosine phosphatases in the human genome. Cell. 2004;117(6):699–711.
Andersen JN, Elson A, Lammers R, Romer J, Clausen JT, Moller KB, et al. Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling. Biochem J. 2001a;354(Pt 3):581–90.
Andersen JN, Mortensen OH, Peters GH, Drake PG, Iversen LF, Olsen OH, et al. Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol Cell Biol. 2001b;21(21):7117–36.
Berman-Golan D, Elson A. Neu-mediated phosphorylation of protein tyrosine phosphatase epsilon is critical for activation of Src in mammary tumor cells. Oncogene. 2007;26(49):7028–37.
De Franceschi L, Biondani A, Carta F, Turrini F, Laudanna C, Deana R, et al. PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells. Proteomics. 2008;8(22):4695–708.
den Hertog J, Ostman A, Bohmer FD. Protein tyrosine phosphatases: regulatory mechanisms. FEBS J. 2008;275(5):831–47.
Elson A. Protein tyrosine phosphatase epsilon increases the risk of mammary hyperplasia and mammary tumors in transgenic mice. Oncogene. 1999;18(52):7535–42.
Elson A, Leder P. Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon. Proc Natl Acad Sci USA. 1995a;92(26):12235–9.
Elson A, Leder P. Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu. J Biol Chem. 1995b;270(44):26116–22.
Gil-Henn H, Elson A. Tyrosine phosphatase-epsilon activates Src and supports the transformed phenotype of Neu-induced mammary tumor cells. J Biol Chem. 2003;278(18):15579–86.
Gil-Henn H, Volohonsky G, Toledano-Katchalski H, Gandre S, Elson A. Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. Oncogene. 2000;19(38):4375–84.
Gil-Henn H, Volohonsky G, Elson A. Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage. J Biol Chem. 2001;276(34):31772–9.
Granot-Attas S, Luxenburg C, Finkelshtein E, Elson A. PTP epsilon regulates integrin-mediated podosome stability in osteoclasts by activating src. Mol Biol Cell. 2009;20(20):4324–34.
Hendriks WJ, Elson A, Harroch S, Stoker AW. Protein tyrosine phosphatases: functional inferences from mouse models and human diseases. FEBS J. 2008;275(5):816–30.
Krueger NX, Streuli M, Saito H. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 1990;9:3241–52.
Muja N, Lovas G, Romm E, Machleder D, Ranjan M, Gallo V, et al. Expression of a catalytically inactive transmembrane protein tyrosine phosphatase epsilon (tm-PTP epsilon) delays optic nerve myelination. Glia. 2004;48(4):278–97.
Nakagawa Y, Yamada N, Shimizu H, Shiota M, Tamura M, Kim-Mitsuyama S, et al. Tyrosine phosphatase epsilonM stimulates migration and survival of porcine aortic endothelial cells by activating c-Src. Biochem Biophys Res Commun. 2004;325(1):314–9.
Nakagawa Y, Aoki N, Aoyama K, Shimizu H, Shimano H, Yamada N, et al. Receptor-type protein tyrosine phosphatase epsilon (PTPepsilonM) is a negative regulator of insulin signaling in primary hepatocytes and liver. Zool Sci. 2005;22(2):169–75.
Nakamura K, Mizuno Y, Kikuchi K. Molecular cloning of a novel cytoplasmic protein tyrosine phosphatase PTP epsilon. Biochem Biophys Res Commun. 1996;218:726–32.
Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A. Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. EMBO J. 2000;19:4036–45.
Rousso-Noori L, Knobler H, Levy-Apter E, Kuperman Y, Neufeld-Cohen A, Keshet Y, et al. Protein tyrosine phosphatase epsilon affects body weight by downregulating leptin signaling in a phosphorylation-dependent manner. Cell Metab. 2011;13(5):562–72.
Sines T, Granot-Attas S, Weisman-Welcher S, Elson A. Association of tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor. Mol Cell Biol. 2007;27(20):7102–12.
Sully V, Pownall S, Vincan E, Bassal S, Borowski AH, Hart PH, et al. Functional abnormalities in protein tyrosine phosphatase epsilon-deficient macrophages. Biochem Biophys Res Commun. 2001;286:184–8.
Tanuma N, Nakamura K, Kikuchi K. Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation. Eur J Biochem. 1999;259:46–54.
Tanuma N, Shima H, Nakamura K, Kikuchi K. Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin- 10-induced JAK-STAT signaling. Blood. 2001;98:3030–4.
Tanuma N, Shima H, Shimada S, Kikuchi K. Reduced tumorigenicity of murine leukemia cells expressing protein-tyrosine phosphatase, PTPepsilon C. Oncogene. 2003;22(12):1758–62.
Thompson LJ, Jiang J, Madamanchi N, Runge MS, Patterson C. PTP-epsilon, a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation. Am J Physiol Heart Circ Physiol. 2001;281:H396–403.
Toledano-Katchalski H, Tiran Z, Sines T, Shani G, Granot-Attas S, den Hertog J, et al. Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon. Mol Cell Biol. 2003;23(15):5460–71.
Tonks NK. Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol. 2006;7(11):833–46.
Wabakken T, Hauge H, Funderud S, Aasheim HC. Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform. Scand J Immunol. 2002;56(3):276–85.
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Elson, A., Rousso-Noori, L. (2018). PTPe (RPTPe and Cyt-PTPe). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_525
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DOI: https://doi.org/10.1007/978-3-319-67199-4_525
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