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Volumn 281, Issue 2, 2002, Pages 182-189

Nuclear localization of non-receptor protein tyrosine phosphatase ε is regulated by its unique N-terminal domain

Author keywords

Hydrogen peroxide; Nuclear localization signal; Oxidative stress; Tyrosine phosphatase

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE;

EID: 0037002187     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5661     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks, N. K., and Neel, B. G. (2001). Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell Biol 13, 182-195.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 2
    • 0033167111 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases in development
    • den Hertog, J. (1999). Protein-tyrosine phosphatases in development. Mech. Dev. 85, 3-14.
    • (1999) Mech. Dev. , vol.85 , pp. 3-14
    • Den Hertog, J.1
  • 3
    • 0033858043 scopus 로고    scopus 로고
    • Emerging issues in receptor protein tyrosine phosphatase function: Lifting fog or simply shifting?
    • Petrone, A., and Sap, J. (2000). Emerging issues in receptor protein tyrosine phosphatase function: Lifting fog or simply shifting? J. Cell Sci. 113, 2345-2354.
    • (2000) J. Cell Sci. , vol.113 , pp. 2345-2354
    • Petrone, A.1    Sap, J.2
  • 5
    • 0028299432 scopus 로고
    • "Zip codes" direct intra-cellular protein tyrosine phosphatases to the correct cellular "address"
    • Mauro, L. J., and Dixon, J. E. (1994). "Zip codes" direct intra-cellular protein tyrosine phosphatases to the correct cellular "address". Trends Biochem. Sci. 19, 151-155.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 151-155
    • Mauro, L.J.1    Dixon, J.E.2
  • 6
    • 0032877635 scopus 로고    scopus 로고
    • Cell signaling by protein tyrosine phosphorylation
    • Fischer, E. H. (1999). Cell signaling by protein tyrosine phosphorylation. Adv. Enzyme Regul. 39, 359-369.
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 359-369
    • Fischer, E.H.1
  • 7
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets
    • Frangioni, J. V., Oda, A., Smith, M., Salzman, E. W., and Neel, B. G. (1993). Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets. EMBO J. 12, 4843-4856.
    • (1993) EMBO J. , vol.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3    Salzman, E.W.4    Neel, B.G.5
  • 8
    • 0029958610 scopus 로고    scopus 로고
    • The properties of the protein tyrosine phosphatase PTPMEG
    • Gu, M., and Majerus, P. W. (1996). The properties of the protein tyrosine phosphatase PTPMEG. J. Biol. Chem. 271, 27751-27759.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27751-27759
    • Gu, M.1    Majerus, P.W.2
  • 9
    • 0032742620 scopus 로고    scopus 로고
    • Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of striatal enriched tyrosine phospha-tase (STEP)
    • Gurd, J. W., Bissoon, N., Nguyen, T. H., Lombroso, P. J., Rider, C. C., Beesley, P. W., and Vannucci, S. J. (1999). Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of striatal enriched tyrosine phospha-tase (STEP). J. Neurochem. 73, 1990-1994.
    • (1999) J. Neurochem. , vol.73 , pp. 1990-1994
    • Gurd, J.W.1    Bissoon, N.2    Nguyen, T.H.3    Lombroso, P.J.4    Rider, C.C.5    Beesley, P.W.6    Vannucci, S.J.7
  • 10
    • 0032692172 scopus 로고    scopus 로고
    • Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP)
    • Nguyen, T. H., Paul, S., Xu, Y., Gurd, J. W., and Lombroso, P. J. (1999). Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP). J. Neurochem. 73, 1995-2001.
    • (1999) J. Neurochem. , vol.73 , pp. 1995-2001
    • Nguyen, T.H.1    Paul, S.2    Xu, Y.3    Gurd, J.W.4    Lombroso, P.J.5
  • 11
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G., and Bastiaens, P. I. (2002). Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295, 1708-1711.
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 12
    • 0031455169 scopus 로고    scopus 로고
    • Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events
    • Rock, M. T., Brooks, W. H., and Roszman, T. L. (1997). Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events. J. Biol. Chem. 272, 33377-33383.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33377-33383
    • Rock, M.T.1    Brooks, W.H.2    Roszman, T.L.3
  • 14
    • 0030024641 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase epsilon gene maps to mouse chromosome 7 and human chromosome 10q26
    • Elson, A., Kozak., C. A., Morton, C. C., Weremowicz, S., and Leder, P. (1996). The protein tyrosine phosphatase epsilon gene maps to mouse chromosome 7 and human chromosome 10q26. Genomics 31, 373-375.
    • (1996) Genomics , vol.31 , pp. 373-375
    • Elson, A.1    Kozak, C.A.2    Morton, C.C.3    Weremowicz, S.4    Leder, P.5
  • 15
    • 0033556074 scopus 로고    scopus 로고
    • Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation
    • Tanuma, N., Nakamura, K., and Kikuchi, K. (1999). Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation. Eur. J. Biochem. 259, 46-54.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 46-54
    • Tanuma, N.1    Nakamura, K.2    Kikuchi, K.3
  • 16
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Krueger, N. X., Streuli, M., and Saito, H. (1990). Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 9, 3241-3252.
    • (1990) EMBO J. , vol.9 , pp. 3241-3252
    • Krueger, N.X.1    Streuli, M.2    Saito, H.3
  • 17
    • 0028970558 scopus 로고
    • Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras or neu
    • Elson, A. & Leder, P. (1995). Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras or neu. J. Biol. Chem. 270, 26116-26122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26116-26122
    • Elson, A.1    Leder, P.2
  • 18
    • 0033539893 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase ε increases the risk of mammary hyperplasia and mammary tumors in transgenic mice
    • Elson, A. (1999). Protein tyrosine phosphatase ε increases the risk of mammary hyperplasia and mammary tumors in transgenic mice. Oncogene 18, 7535-7542.
    • (1999) Oncogene , vol.18 , pp. 7535-7542
    • Elson, A.1
  • 19
  • 20
    • 0035868264 scopus 로고    scopus 로고
    • Comparative study of PTP3 isoforms: Membrane localization confers specificity in inhibiting insulin-induced cell rounding and cell detatchment
    • Andersen, J. N., Elson, A., Lammers, R., Romer, J., Clausen, J. T., Moller, K. B., and Moller, N. P. H. (2001). Comparative study of PTP3 isoforms: Membrane localization confers specificity in inhibiting insulin-induced cell rounding and cell detatchment. Biochem. J. 354, 581-590.
    • (2001) Biochem. J. , vol.354 , pp. 581-590
    • Andersen, J.N.1    Elson, A.2    Lammers, R.3    Romer, J.4    Clausen, J.T.5    Moller, K.B.6    Moller, N.P.H.7
  • 21
    • 0029583853 scopus 로고
    • Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon
    • Elson, A., and Leder, P. (1995). Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon. Proc. Natl. Acad. Sci. USA. 92, 12235-12239.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12235-12239
    • Elson, A.1    Leder, P.2
  • 22
    • 0030068389 scopus 로고    scopus 로고
    • Molecular cloning of a novel cytoplasmic protein tyrosine phosphatase PTP epsilon
    • Nakamura, K., Mizuno, Y., and Kikuchi, K. (1996). Molecular cloning of a novel cytoplasmic protein tyrosine phosphatase PTP epsilon. Biochem. Biophys. Res. Commun. 218, 726-732.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 726-732
    • Nakamura, K.1    Mizuno, Y.2    Kikuchi, K.3
  • 23
    • 0034618404 scopus 로고    scopus 로고
    • Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control
    • Gil-Henn, H., Volohonsky, G., Toledano-Katchalski, H., Gandre, S., and Elson, A. (2000). Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control. Oncogene 19, 4375-4384.
    • (2000) Oncogene , vol.19 , pp. 4375-4384
    • Gil-Henn, H.1    Volohonsky, G.2    Toledano-Katchalski, H.3    Gandre, S.4    Elson, A.5
  • 24
    • 0034254725 scopus 로고    scopus 로고
    • Hypomyelination and increased activity of voltage-gated potassium channels in mice lacking protein tyrosine phosphatase ε
    • Peretz, A., Gil-Henn, H., Sobko, A., Shinder, V., Attali, B., and Elson, A. (2000). Hypomyelination and increased activity of voltage-gated potassium channels in mice lacking protein tyrosine phosphatase ε. EMBO J. 19, 4036-4045.
    • (2000) EMBO J. , vol.19 , pp. 4036-4045
    • Peretz, A.1    Gil-Henn, H.2    Sobko, A.3    Shinder, V.4    Attali, B.5    Elson, A.6
  • 25
    • 0035943706 scopus 로고    scopus 로고
    • Regulation of RPTP alpha and PTP epsilon by calpain-mediated proteolytic cleavage
    • Gil-Henn, H., Volohonsky, G., and Elson, A. (2001). Regulation of RPTP alpha and PTP epsilon by calpain-mediated proteolytic cleavage. J. Biol. Chem. 276, 31772-31779.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31772-31779
    • Gil-Henn, H.1    Volohonsky, G.2    Elson, A.3
  • 26
    • 0034803339 scopus 로고    scopus 로고
    • PTP-epsilon, a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation
    • Thompson, L. J., Jiang, J., Madamanchi, N., Runge, M. S., and Patterson, C. (2001). PTP-epsilon, a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation. Am. J. Physiol. Heart Circ. Physiol. 281, H396-403.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Thompson, L.J.1    Jiang, J.2    Madamanchi, N.3    Runge, M.S.4    Patterson, C.5
  • 28
    • 0034623287 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase PTP epsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells
    • Tanuma, N., Nakamura, K., Shima, H., and Kikuchi, K. (2000). Protein-tyrosine phosphatase PTP epsilon C inhibits Jak-STAT signaling and differentiation induced by interleukin-6 and leukemia inhibitory factor in M1 leukemia cells. J. Biol. Chem. 275, 28216-28221.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28216-28221
    • Tanuma, N.1    Nakamura, K.2    Shima, H.3    Kikuchi, K.4
  • 29
    • 0035892127 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilon C selectively inhibits interleukin 6- and interleukin 10-induced JAK-STAT signaling
    • Tanuma, N., Shima, H., Nakamura, K., and Kikuchi, K. (2001). Protein tyrosine phosphatase epsilon C selectively inhibits interleukin 6- and interleukin 10-induced JAK-STAT signaling. Blood 98, 3030-3034.
    • (2001) Blood , vol.98 , pp. 3030-3034
    • Tanuma, N.1    Shima, H.2    Nakamura, K.3    Kikuchi, K.4
  • 30
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and Okayama, H. (1987). High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 31
    • 0033625442 scopus 로고    scopus 로고
    • Nuclear targeting of proteins: How many different signals?
    • Christophe, D., Christophe-Hobertus, C., and Pichon, B. (2000). Nuclear targeting of proteins: How many different signals? Cell Signal. 12, 337-341.
    • (2000) Cell Signal , vol.12 , pp. 337-341
    • Christophe, D.1    Christophe-Hobertus, C.2    Pichon, B.3
  • 32
    • 0036196670 scopus 로고    scopus 로고
    • Protein and RNA export from the nucleus
    • Lei, E. P., and Silver, P. A. (2002). Protein and RNA export from the nucleus. Dev. Cell 2, 261-272.
    • (2002) Dev. Cell , vol.2 , pp. 261-272
    • Lei, E.P.1    Silver, P.A.2
  • 33
    • 0034669111 scopus 로고    scopus 로고
    • Nuclear export signal located within the DNA-binding domain of the STAT1 transcription factor
    • McBride, K. M., McDonald, C., and Reich, N. C. (2000). Nuclear export signal located within the DNA-binding domain of the STAT1 transcription factor. EMBO J. 19, 6196-6206.
    • (2000) EMBO J. , vol.19 , pp. 6196-6206
    • McBride, K.M.1    McDonald, C.2    Reich, N.C.3
  • 34
    • 0035918217 scopus 로고    scopus 로고
    • Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C lambda
    • Perander, M., Bjorkoy, G., and Johansen, T. (2001). Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C lambda. J. Biol. Chem. 276, 13015-130124.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13015-130124
    • Perander, M.1    Bjorkoy, G.2    Johansen, T.3
  • 35
    • 0035813144 scopus 로고    scopus 로고
    • Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP
    • Lam, M. H., Michell, B. J., Fodero-Tavoletti, M. T., Kemp, B. E., Tonks, N. K., and Tiganis, T. (2001). Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP. J. Biol. Chem. 276, 37700-37707.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37700-37707
    • Lam, M.H.1    Michell, B.J.2    Fodero-Tavoletti, M.T.3    Kemp, B.E.4    Tonks, N.K.5    Tiganis, T.6
  • 36
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson, B. R., and Eleftheriou, A. (2000). A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256, 213-224.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 38
    • 0037084009 scopus 로고    scopus 로고
    • Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress
    • Blanchetot, C., Tertoolen, L. G., and den Hertog, J. (2002). Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress. EMBO J. 21, 493-503.
    • (2002) EMBO J. , vol.21 , pp. 493-503
    • Blanchetot, C.1    Tertoolen, L.G.2    Den Hertog, J.3
  • 39
    • 0036467477 scopus 로고    scopus 로고
    • Apoptosis and tumourigenesis
    • Hickman, J. A. (2002). Apoptosis and tumourigenesis. Curr. Opin. Genet. Dev. 12, 67-72.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 67-72
    • Hickman, J.A.1
  • 40
    • 0031911792 scopus 로고    scopus 로고
    • ZIP kinase, a novel serine/threonine kinase which mediates apoptosis
    • Kawai, T. Matsumoto, M., Takeda, K., Sanjo, H., and Akira, S. (1998). ZIP kinase, a novel serine/threonine kinase which mediates apoptosis. Mol. Cell. Biol. 18, 1642-1651.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1642-1651
    • Kawai, T.1    Matsumoto, M.2    Takeda, K.3    Sanjo, H.4    Akira, S.5
  • 41
    • 0031056002 scopus 로고    scopus 로고
    • DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • Cohen, O., Feinstein, E., and Kimchi, A. (1997). DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 16, 998-1008.
    • (1997) EMBO J. , vol.16 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3


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