메뉴 건너뛰기




Volumn 17, Issue 10, 2006, Pages 4330-4342

Tyrosine phosphatases ε and α perform specific and overlapping functions in regulation of voltage-gated potassium channels in Schwann cells

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE ALPHA; PROTEIN TYROSINE PHOSPHATASE EPSILON; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; SHAB POTASSIUM CHANNEL;

EID: 33749485651     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-02-0151     Document Type: Article
Times cited : (25)

References (71)
  • 2
    • 0035868264 scopus 로고    scopus 로고
    • Comparative study of protein tyrosine phosphatase-epsilon isoforms: Membrane localization confers specificity in cellular signalling
    • Andersen, J. N., Elson, A., Lammers, R., Romer, J., Clausen, J. T., Moller, K. B., and Moller, N. P. (2001). Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling. 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.7
  • 4
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge, J. D., Pang, A., and Fujita, D. J. (2000). Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275, 41439-41446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 5
    • 10644268691 scopus 로고    scopus 로고
    • Substrate-trapping techniques in the identification of cellular PTP targets
    • Blanchetot, C., Chagnon, M., Dube, N., Halle, M., and Tremblay, M. L. (2005). Substrate-trapping techniques in the identification of cellular PTP targets. Methods 35, 44-53.
    • (2005) Methods , vol.35 , pp. 44-53
    • Blanchetot, C.1    Chagnon, M.2    Dube, N.3    Halle, M.4    Tremblay, M.L.5
  • 9
    • 0030974135 scopus 로고    scopus 로고
    • Competition and cooperation among receptor tyrosine phosphatases control motoneuron growth cone guidance in Drosophila
    • Desai, C. J., Krueger, N. X., Saito, H., and Zinn, K. (1997). Competition and cooperation among receptor tyrosine phosphatases control motoneuron growth cone guidance in Drosophila. Development 124, 1941-1952.
    • (1997) Development , vol.124 , pp. 1941-1952
    • Desai, C.J.1    Krueger, N.X.2    Saito, H.3    Zinn, K.4
  • 10
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly, M., et al. (1999). Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283, 1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 11
    • 0029583853 scopus 로고
    • Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon
    • Elson, A., and Leder, P. (1995a). 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
  • 12
    • 0028970558 scopus 로고
    • Protein-tyrosine phosphatase epsiloh. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras or neu
    • Elson, A., and Leder, P. (1995b). Protein-tyrosine phosphatase epsiloh. 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
  • 13
    • 0030777123 scopus 로고    scopus 로고
    • Tyrosine phosphorylation modulates current amplitude and kinetics of a neuronal voltage-gated potassium channel
    • Fadool, D. A., Holmes, T. C., Berman, K., Dagan, D., and Levitan, I. B. (1997). Tyrosine phosphorylation modulates current amplitude and kinetics of a neuronal voltage-gated potassium channel. J. Neurophysiol. 78, 1563-1573.
    • (1997) J. Neurophysiol. , vol.78 , pp. 1563-1573
    • Fadool, D.A.1    Holmes, T.C.2    Berman, K.3    Dagan, D.4    Levitan, I.B.5
  • 14
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint, A. J., Tiganis, T., Barford, D., and Tonks, N. K. (1997). Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 94, 1680-1685.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 15
    • 0037844867 scopus 로고    scopus 로고
    • Tyrosine phosphatase-epsilon activates Src and supports the transformed phenotype of Neu-induced mammary tumor cells
    • Gil-Henn, H., and Elson, A. (2003). Tyrosine phosphatase-epsilon activates Src and supports the transformed phenotype of Neu-induced mammary tumor cells. J. Biol. Chem. 278, 15579-15586.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15579-15586
    • Gil-Henn, H.1    Elson, A.2
  • 16
    • 0035943706 scopus 로고    scopus 로고
    • Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage
    • Gil-Henn, H., Volohonsky, G., and Elson, A. (2001). Regulation of protein-tyrosine phosphatases alpha and 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
  • 17
    • 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
  • 18
    • 1242316972 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilon activates Yes and Fyn in Neu-induced mammary tumor cells
    • Granot-Attas, S., and Elson, A. (2004). Protein tyrosine phosphatase epsilon activates Yes and Fyn in Neu-induced mammary tumor cells. Exp. Cell Res. 294, 236-243.
    • (2004) Exp. Cell Res. , vol.294 , pp. 236-243
    • Granot-Attas, S.1    Elson, A.2
  • 19
    • 0036842987 scopus 로고    scopus 로고
    • A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions
    • Harroch, S., Furtado, G. C., Brueck, W., Rosenbluth, J., Lafaille, J., Chao, M., Buxbaum, J. D., and Schlessinger, J. (2002). A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions. Nat. Genet. 32, 411-414.
    • (2002) Nat. Genet. , vol.32 , pp. 411-414
    • Harroch, S.1    Furtado, G.C.2    Brueck, W.3    Rosenbluth, J.4    Lafaille, J.5    Chao, M.6    Buxbaum, J.D.7    Schlessinger, J.8
  • 20
    • 0034495964 scopus 로고    scopus 로고
    • Role of receptor protein tyrosine phosphatase alpha (RPTPalpha) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels
    • Imbrici, P., Tucker, S. J., D'Adamo, M. C., and Pessia, M. (2000). Role of receptor protein tyrosine phosphatase alpha (RPTPalpha) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels. Pflueg. Arch. Eur. J. Physiol. 441, 257-262.
    • (2000) Pflueg. Arch. Eur. J. Physiol. , vol.441 , pp. 257-262
    • Imbrici, P.1    Tucker, S.J.2    D'Adamo, M.C.3    Pessia, M.4
  • 21
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman, L. D., et al (2000). Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20, 5479-5489.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1
  • 22
    • 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
  • 23
    • 15744384803 scopus 로고    scopus 로고
    • Interaction of the insulin receptor with the receptor-like protein tyrosine phosphatases PTPalpha and PTPepsilon in living cells
    • Lacasa, D., Boute, N., and Issad, T. (2005). Interaction of the insulin receptor with the receptor-like protein tyrosine phosphatases PTPalpha and PTPepsilon in living cells. Mol. Pharmacol. 67, 1206-1213.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1206-1213
    • Lacasa, D.1    Boute, N.2    Issad, T.3
  • 24
    • 0031035983 scopus 로고    scopus 로고
    • The transmembrane protein tyrosine phosphatase alpha dephosphorylates the insulin receptor in intact cells
    • Lammers, R., Moller, N. P., and Ullrich, A. (1997). The transmembrane protein tyrosine phosphatase alpha dephosphorylates the insulin receptor in intact cells. FEBS Lett. 404, 37-40.
    • (1997) FEBS Lett. , vol.404 , pp. 37-40
    • Lammers, R.1    Moller, N.P.2    Ullrich, A.3
  • 25
    • 0347004670 scopus 로고    scopus 로고
    • Insulin signaling and glucose homeostasis in mice lacking protein tyrosine phosphatase alpha
    • Le, H. T., Ponniah, S., and Pallen, C. J. (2004). Insulin signaling and glucose homeostasis in mice lacking protein tyrosine phosphatase alpha. Biochem. Biophys. Res. Commun. 314, 321-329.
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 321-329
    • Le, H.T.1    Ponniah, S.2    Pallen, C.J.3
  • 26
    • 0032616958 scopus 로고    scopus 로고
    • Modulation of ion channels by protein phosphorylation. How the brain works
    • Levitan, I. B. (1999). Modulation of ion channels by protein phosphorylation. How the brain works. Adv. Second Messenger Phosphoprotein Res. 33, 3-22.
    • (1999) Adv. Second Messenger Phosphoprotein Res. , vol.33 , pp. 3-22
    • Levitan, I.B.1
  • 27
    • 0034662325 scopus 로고    scopus 로고
    • Modulation of Kv1.5 currents by Src tyrosine phosphorylation: Potential role in the differentiation of astrocytes
    • MacFarlane, S. N., and Sontheimer, H. (2000). Modulation of Kv1.5 currents by Src tyrosine phosphorylation: potential role in the differentiation of astrocytes. J. Neurosci. 20, 5245-5253.
    • (2000) J. Neurosci. , vol.20 , pp. 5245-5253
    • MacFarlane, S.N.1    Sontheimer, H.2
  • 29
    • 0033292933 scopus 로고    scopus 로고
    • Modulation of Kv channel alpha/beta subunit interactions
    • Martens, J. R., Kwak, Y. G., and Tamkun, M. M. (1999). Modulation of Kv channel alpha/beta subunit interactions. Trends Cardiovasc. Med. 9, 253-258.
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 253-258
    • Martens, J.R.1    Kwak, Y.G.2    Tamkun, M.M.3
  • 30
    • 3042842349 scopus 로고    scopus 로고
    • Dysmyelination and reduced myelin basic protein gene expression by oligodendrocytes of SHP-1-deficient mice
    • Massa, P. T., Wu, C., and Fecenko-Tacka, K. (2004). Dysmyelination and reduced myelin basic protein gene expression by oligodendrocytes of SHP-1-deficient mice. J. Neurosci. Res. 77, 15-25.
    • (2004) J. Neurosci. Res. , vol.77 , pp. 15-25
    • Massa, P.T.1    Wu, C.2    Fecenko-Tacka, K.3
  • 31
    • 30644461158 scopus 로고    scopus 로고
    • Calcium- and metabolic state-dependent modulation of the voltage-dependent Kv2.1 channel regulates neuronal excitability in response to ischemia
    • Misonou, H., Mohapatra, D. P., Menegola, M., and Trimmer, J. S. (2005). Calcium- and metabolic state-dependent modulation of the voltage-dependent Kv2.1 channel regulates neuronal excitability in response to ischemia. J. Neurosci. 25, 11184-11193.
    • (2005) J. Neurosci. , vol.25 , pp. 11184-11193
    • Misonou, H.1    Mohapatra, D.P.2    Menegola, M.3    Trimmer, J.S.4
  • 33
  • 34
    • 18044380363 scopus 로고    scopus 로고
    • Receptor-type protein tyrosine phosphatase epsilon (PTPepsilonM) is a negative regulator of insulin signaling in primary hepatocytes and liver
    • Nakagawa, Y., Aoki, N., Aoyama, K., Shimizu, H., Shimano, H., Yamada, N., and Miyazaki, H. (2005). Receptor-type protein tyrosine phosphatase epsilon (PTPepsilonM) is a negative regulator of insulin signaling in primary hepatocytes and liver. Zoolog. Sci. 22, 169-175.
    • (2005) Zoolog. Sci. , vol.22 , pp. 169-175
    • Nakagawa, Y.1    Aoki, N.2    Aoyama, K.3    Shimizu, H.4    Shimano, H.5    Yamada, N.6    Miyazaki, H.7
  • 36
    • 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
  • 37
    • 0037647185 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha (PTPalpha): A Src family kinase activator and mediator of multiple biological effects
    • Pallen, C. J. (2003). Protein tyrosine phosphatase alpha (PTPalpha): a Src family kinase activator and mediator of multiple biological effects. Curr. Top. Med. Chem. 3, 821-835.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 821-835
    • Pallen, C.J.1
  • 38
    • 0030800121 scopus 로고    scopus 로고
    • The motheaten mutation rescues B cell signaling and development in CD45-deficient mice
    • Pani, G., Siminovitch, K. A., and Paige, C. J. (1997). The motheaten mutation rescues B cell signaling and development in CD45-deficient mice. J. Exp. Med. 186, 581-588.
    • (1997) J. Exp. Med. , vol.186 , pp. 581-588
    • Pani, G.1    Siminovitch, K.A.2    Paige, C.J.3
  • 39
    • 0034254725 scopus 로고    scopus 로고
    • Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon
    • Peretz, A., Gil-Henn, H., Sobko, A., Shinder, V., Attali, B., and Elson, A. (2000). Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. 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
  • 40
    • 0033198485 scopus 로고    scopus 로고
    • Tyrosine kinases modulate K+ channel gating in mouse Schwann cells
    • Peretz, A., Sobko, A., and Attali, B. (1999). Tyrosine kinases modulate K+ channel gating in mouse Schwann cells. J. Physiol. 519, 373-384.
    • (1999) J. Physiol. , vol.519 , pp. 373-384
    • Peretz, A.1    Sobko, A.2    Attali, B.3
  • 41
  • 42
    • 0029038677 scopus 로고
    • Regulation of the activity of voltage-gated potassium channels by beta subunits
    • Pongs, O. (1995). Regulation of the activity of voltage-gated potassium channels by beta subunits. Semin. Neurosci. 7, 137-146.
    • (1995) Semin. Neurosci. , vol.7 , pp. 137-146
    • Pongs, O.1
  • 43
    • 0033587177 scopus 로고    scopus 로고
    • Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn
    • Ponniah, S., Wang, D. Z., Lim, K. L., and Pallen, C. J. (1999). Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn. Curr. Biol. 9, 535-538.
    • (1999) Curr. Biol. , vol.9 , pp. 535-538
    • Ponniah, S.1    Wang, D.Z.2    Lim, K.L.3    Pallen, C.J.4
  • 45
    • 0035164751 scopus 로고    scopus 로고
    • Regulation of CNS and motor axon guidance in Drosophila by the receptor tyrosine phosphatase DPTP52F
    • Schindelholz, B., Knirr, M., Warrior, R., and Zinn, K. (2001). Regulation of CNS and motor axon guidance in Drosophila by the receptor tyrosine phosphatase DPTP52F. Development 128, 4371-4382.
    • (2001) Development , vol.128 , pp. 4371-4382
    • Schindelholz, B.1    Knirr, M.2    Warrior, R.3    Zinn, K.4
  • 46
    • 0041655974 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha (PTP alpha) knockout mice show deficits in Morris water maze learning, decreased locomotor activity, and decreases in anxiety
    • Skelton, M. R., Ponniah, S., Wang, D. Z., Doetschman, T., Vorhees, C. V., and Pallen, C. J. (2003). Protein tyrosine phosphatase alpha (PTP alpha) knockout mice show deficits in Morris water maze learning, decreased locomotor activity, and decreases in anxiety. Brain Res. 984, 1-10.
    • (2003) Brain Res. , vol.984 , pp. 1-10
    • Skelton, M.R.1    Ponniah, S.2    Wang, D.Z.3    Doetschman, T.4    Vorhees, C.V.5    Pallen, C.J.6
  • 47
    • 0032541410 scopus 로고    scopus 로고
    • Constitutive activation of delayed-rectifier potassium channels by a src family tyrosine kinase in Schwann cells
    • Sobko, A., Peretz, A., and Attali, B. (1998a). Constitutive activation of delayed-rectifier potassium channels by a src family tyrosine kinase in Schwann cells. EMBO J. 17, 4723-4734.
    • (1998) EMBO J. , vol.17 , pp. 4723-4734
    • Sobko, A.1    Peretz, A.2    Attali, B.3
  • 48
    • 0032535702 scopus 로고    scopus 로고
    • Heteromultimeric delayed-rectifier K+ channels in sSchwann cells: Developmental expression and role in cell proliferation
    • Sobko, A., Peretz, A., Shirihai, O., Etkin, S., Cherepanova, V., Dagan, D., and Attali, B. (1998b). Heteromultimeric delayed-rectifier K+ channels in sSchwann cells: developmental expression and role in cell proliferation. J. Neurosci. 18, 10398-10408.
    • (1998) J. Neurosci. , vol.18 , pp. 10398-10408
    • Sobko, A.1    Peretz, A.2    Shirihai, O.3    Etkin, S.4    Cherepanova, V.5    Dagan, D.6    Attali, B.7
  • 49
    • 0030868305 scopus 로고    scopus 로고
    • Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase
    • Somani, A. K., Bignon, J. S., Mills, G. B., Siminovitch, K. A., and Branch, D. R. (1997). Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase. J. Biol. Chem. 272, 21113-21119.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21113-21119
    • Somani, A.K.1    Bignon, J.S.2    Mills, G.B.3    Siminovitch, K.A.4    Branch, D.R.5
  • 50
    • 17644403551 scopus 로고    scopus 로고
    • Receptor tyrosine phosphatases guide vertebrate motor axons during development
    • Stepanek, L., Stoker, A. W., Stoeckli, E., and Bixby, J. L. (2005). Receptor tyrosine phosphatases guide vertebrate motor axons during development. J. Neurosci. 25, 3813-3823.
    • (2005) J. Neurosci. , vol.25 , pp. 3813-3823
    • Stepanek, L.1    Stoker, A.W.2    Stoeckli, E.3    Bixby, J.L.4
  • 51
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su, J., Muranjan, M., and Sap, J. (1999). Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 9, 505-511.
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 53
    • 0035114432 scopus 로고    scopus 로고
    • Complex genetic interactions among four receptor tyrosine phosphatases regulate axon guidance in Drosophila
    • Sun, Q., Schindelholz, B., Knirr, M., Schmid, A., and Zinn, K. (2001). Complex genetic interactions among four receptor tyrosine phosphatases regulate axon guidance in Drosophila. Mol. Cell. Neurosci. 17, 274-291.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 274-291
    • Sun, Q.1    Schindelholz, B.2    Knirr, M.3    Schmid, A.4    Zinn, K.5
  • 54
    • 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
  • 55
    • 0034623287 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase PTPepsilon 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 PTPepsilon 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
  • 56
    • 0035892127 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin-10-induced JAK-STAT signaling
    • Tanuma, N., Shima, H., Nakamura, K., and Kikuchi, K. (2001). Protein tyrosine phosphatase epsilonC 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
  • 57
    • 0037468571 scopus 로고    scopus 로고
    • Reduced tumorigenicity of murine leukemia cells expressing protein-tyrosine phosphatase, PTPepsilon C
    • Tanuma, N., Shima, H., Shimada, S., and Kikuchi, K. (2003). Reduced tumorigenicity of murine leukemia cells expressing protein-tyrosine phosphatase, PTPepsilon C. Oncogene 22, 1758-1762.
    • (2003) Oncogene , vol.22 , pp. 1758-1762
    • Tanuma, N.1    Shima, H.2    Shimada, S.3    Kikuchi, K.4
  • 58
    • 0037930864 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon
    • Tiran, Z., Peretz, A., Attali, B., and Elson, A. (2003). Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase epsilon. J. Biol. Chem. 278, 17509-17514.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17509-17514
    • Tiran, Z.1    Peretz, A.2    Attali, B.3    Elson, A.4
  • 60
    • 0025787869 scopus 로고
    • Immunological identification and characterization of a delayed rectifier K+ channel polypeptide in rat brain
    • Trimmer, J. S. (1991). Immunological identification and characterization of a delayed rectifier K+ channel polypeptide in rat brain. Proc. Natl. Acad. Sci. USA 88, 10764-10768.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10764-10768
    • Trimmer, J.S.1
  • 61
    • 0033521647 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity
    • Tsai, W., Morielli, A. D., Cachero, T. G., and Peralta, E. G. (1999). Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity. EMBO J. 18, 109-118.
    • (1999) EMBO J. , vol.18 , pp. 109-118
    • Tsai, W.1    Morielli, A.D.2    Cachero, T.G.3    Peralta, E.G.4
  • 62
    • 0025971174 scopus 로고
    • Single K+ channel properties in cultured mouse Schwann cells: Conductance and kinetics
    • Verkhratsky, A., Hoppe, D., and Kettenmann, H. (1991). Single K+ channel properties in cultured mouse Schwann cells: conductance and kinetics. J. Neurosci. Res. 28, 200-209.
    • (1991) J. Neurosci. Res. , vol.28 , pp. 200-209
    • Verkhratsky, A.1    Hoppe, D.2    Kettenmann, H.3
  • 63
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wiehert, G., Jiang, G., Kostic, A., De Vos, K., Sap, J., and Sheetz, M. P. (2003). RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. J. Cell Biol. 161, 143-153.
    • (2003) J. Cell Biol. , vol.161 , pp. 143-153
    • Wiehert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 64
    • 0036065312 scopus 로고    scopus 로고
    • Expression of human protein tyrosine phosphatase epsilon in leucocytes: A potential ERK pathway-regulating phosphatase
    • Wabakken, T., Hauge, H., Finne, E. F., Wiedlocha, A., and Aasheim, H. (2002). Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase. Scand. J. Immunol. 56, 195-203.
    • (2002) Scand. J. Immunol. , vol.56 , pp. 195-203
    • Wabakken, T.1    Hauge, H.2    Finne, E.F.3    Wiedlocha, A.4    Aasheim, H.5
  • 65
    • 0033051169 scopus 로고    scopus 로고
    • Neuronal defects and posterior pituitary hypoplasia in mice lacking the receptor tyrosine phosphatase PTPsigma
    • Wallace, M. J., Batt, J., Fladd, C. A., Henderson, J. T., Skarnes, W., and Rotin, D. (1999). Neuronal defects and posterior pituitary hypoplasia in mice lacking the receptor tyrosine phosphatase PTPsigma. Nat. Genet. 21, 334-338.
    • (1999) Nat. Genet. , vol.21 , pp. 334-338
    • Wallace, M.J.1    Batt, J.2    Fladd, C.A.3    Henderson, J.T.4    Skarnes, W.5    Rotin, D.6
  • 66
    • 0035949479 scopus 로고    scopus 로고
    • Controlling potassium channel activities: Interplay between the membrane and intracellular factors
    • Yi, B. A., Minor, D. L., Jr., Lin, Y. F., Jan, Y. N., and Jan, L. Y. (2001). Controlling potassium channel activities: interplay between the membrane and intracellular factors. Proc. Natl. Acad. Sci. USA 98, 11016-11023.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11016-11023
    • Yi, B.A.1    Minor Jr., D.L.2    Lin, Y.F.3    Jan, Y.N.4    Jan, L.Y.5
  • 67
    • 0033571032 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn
    • Zeng, L., D'Alessandri, L., Kalousek, M. B., Vaughan, L., and Pallen, C. J. (1999). Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn. J. Cell Biol. 147, 707-714.
    • (1999) J. Cell Biol. , vol.147 , pp. 707-714
    • Zeng, L.1    D'Alessandri, L.2    Kalousek, M.B.3    Vaughan, L.4    Pallen, C.J.5
  • 68
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., Si, X., Yu, W. P., Le, H. T., Ng, K. P., Teng, R. M., Ryan, K., Wang, D. Z., Ponniah, S., and Pallen, C. J. (2003). PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160, 137-146.
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 69
    • 8644268830 scopus 로고    scopus 로고
    • Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism
    • Zhang, E. E., Chapeau, E., Hagihara, K., and Feng, G. S. (2004). Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism. Proc. Natl. Acad. Sci. USA 101, 16064-16069.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16064-16069
    • Zhang, E.E.1    Chapeau, E.2    Hagihara, K.3    Feng, G.S.4
  • 70
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng, X. M., Resnick, R. J., and Shalloway, D. (2000). A phosphotyrosine displacement mechanism for activation of Src by PTPalpha. EMBO J. 19, 964-978.
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 71
    • 0030948362 scopus 로고    scopus 로고
    • Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif
    • Zlatkine, P., Mehul, B., and Magee, A. I. (1997). Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif. J. Cell Sci. 110, 673-679.
    • (1997) J. Cell Sci. , vol.110 , pp. 673-679
    • Zlatkine, P.1    Mehul, B.2    Magee, A.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.