메뉴 건너뛰기




Volumn 27, Issue 20, 2007, Pages 7102-7112

Association of tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE PHOSPHATASE EPSILON; TUBULIN; TYROSINE;

EID: 35148892597     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.02096-06     Document Type: Article
Times cited : (20)

References (50)
  • 2
    • 0035868264 scopus 로고    scopus 로고
    • Comparative study of protein tyrosine phosphatase-epsilon isoforms: Membrane localization confers specificity in cellular signalling
    • Andersen, J. N., A. Elson, R. Lammers, J. Romer, J. T. Clausen, K. B. Moller, and N. P. Moller. 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
    • 35148862856 scopus 로고    scopus 로고
    • Neu-mediated phosphorylation of protein tyrosine phosphatase epsilon is critical for activation of Src in mammary tumor cells
    • E-pub ahead of print, doi:10.1038/sj.onc. 1210505
    • Berman-Golan, D., and A. Elson. 2007. Neu-mediated phosphorylation of protein tyrosine phosphatase epsilon is critical for activation of Src in mammary tumor cells. Oncogene [E-pub ahead of print.] doi:10.1038/sj.onc. 1210505.
    • (2007) Oncogene
    • Berman-Golan, D.1    Elson, A.2
  • 5
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C. A., and H. Okayama. 1988. Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6:632-638.
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 6
    • 33744956948 scopus 로고    scopus 로고
    • Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration
    • Chen, M., S. C. Chen, and C. J. Pallen. 2006. Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration. J. Biol. Chem. 281:11972-11980.
    • (2006) J. Biol. Chem , vol.281 , pp. 11972-11980
    • Chen, M.1    Chen, S.C.2    Pallen, C.J.3
  • 8
    • 18944403327 scopus 로고    scopus 로고
    • The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules
    • Cho, H. P., Y. Liu, M. Gomez, J. Dunlap, M. Tyers, and Y. Wang. 2005. The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules. Mol. Cell. Biol. 25:4541-4551.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4541-4551
    • Cho, H.P.1    Liu, Y.2    Gomez, M.3    Dunlap, J.4    Tyers, M.5    Wang, Y.6
  • 9
    • 11144342740 scopus 로고    scopus 로고
    • den Hertog, J., A. Groen, and T. van der Wijk. 2005. Redox regulation of protein-tyrosine phosphatases. Arch. Biochem. Biophys. 434:11-15.
    • den Hertog, J., A. Groen, and T. van der Wijk. 2005. Redox regulation of protein-tyrosine phosphatases. Arch. Biochem. Biophys. 434:11-15.
  • 10
    • 0029583853 scopus 로고
    • Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon
    • Elson, A., and P. Leder. 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
  • 11
    • 0028970558 scopus 로고
    • Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu
    • Elson, A., and P. Leder. 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
  • 12
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint, A. J., T. Tiganis, D. Barford, and N. K. Tonks. 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
  • 13
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets
    • Frangioni, J. V., A. Oda, M. Smith, E. W. Salzman, and B. G. Neel. 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
  • 16
    • 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 A. Elson. 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
  • 17
    • 0035943706 scopus 로고    scopus 로고
    • Regulation of protein-tyrosine phosphatases alpha and epsilon by calpain-mediated proteolytic cleavage
    • Gil-Henn, H., G. Volohonsky, and A. Elson. 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
  • 18
    • 0034618404 scopus 로고    scopus 로고
    • Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control
    • Gil-Henn, H., G. Volohonsky, H. Toledano-Katchalski, S. Gandre, and A. Elson. 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
  • 19
    • 1242316972 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilon activates Yes and Fyn in Neu-induced mammary tumor cells
    • Granot-Attas, S., and A. Elson. 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
  • 20
    • 12244288351 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis
    • Herrmann, L., T. Dittmar, and K. S. Erdmann. 2003. The protein tyrosine phosphatase PTP-BL associates with the midbody and is involved in the regulation of cytokinesis. Mol. Biol. Cell 14:230-240.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 230-240
    • Herrmann, L.1    Dittmar, T.2    Erdmann, K.S.3
  • 21
    • 0024507707 scopus 로고    scopus 로고
    • Himmler, A., D. Drechsel, M. W. Kirschner, and D. W. Martin, Jr. 1989. Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 9:1381-1388.
    • Himmler, A., D. Drechsel, M. W. Kirschner, and D. W. Martin, Jr. 1989. Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol. Cell. Biol. 9:1381-1388.
  • 22
    • 0033859771 scopus 로고    scopus 로고
    • Receptor-like protein tyrosine phosphatase α homodimerizes on the cell surface
    • Jiang, G., J. den Hertog, and T. Hunter. 2000. Receptor-like protein tyrosine phosphatase α homodimerizes on the cell surface. Mol. Cell. Biol. 20:5917-5929.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5917-5929
    • Jiang, G.1    den Hertog, J.2    Hunter, T.3
  • 23
    • 0033533817 scopus 로고    scopus 로고
    • Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
    • Jiang, G., J. den Hertog, J. Su, J. Noel, J. Sap, and T. Hunter. 1999. Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha. Nature 401:606-610.
    • (1999) Nature , vol.401 , pp. 606-610
    • Jiang, G.1    den Hertog, J.2    Su, J.3    Noel, J.4    Sap, J.5    Hunter, T.6
  • 24
    • 0037002187 scopus 로고    scopus 로고
    • Nuclear localization of non-receptor protein tyrosine phosphatase epsilon is regulated by its unique N-terminal domain
    • Kraut, J., G. Volohonsky, H. Toledano-Katchalski, and A. Elson. 2002. Nuclear localization of non-receptor protein tyrosine phosphatase epsilon is regulated by its unique N-terminal domain. Exp. Cell Res. 281:182-189.
    • (2002) Exp. Cell Res , vol.281 , pp. 182-189
    • Kraut, J.1    Volohonsky, G.2    Toledano-Katchalski, H.3    Elson, A.4
  • 25
    • 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., N. Boute, and T. Issad. 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
  • 26
    • 6344242879 scopus 로고    scopus 로고
    • The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly
    • Laurent, C. E., F. J. Delfino, H. Y. Cheng, and T. E. Smithgall. 2004. The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly. Mol. Cell. Biol. 24:9351-9358.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9351-9358
    • Laurent, C.E.1    Delfino, F.J.2    Cheng, H.Y.3    Smithgall, T.E.4
  • 27
    • 0024268202 scopus 로고
    • Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein
    • Lewis, S. A., D. H. Wang, and N. J. Cowan. 1988. Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science 242:936-939.
    • (1988) Science , vol.242 , pp. 936-939
    • Lewis, S.A.1    Wang, D.H.2    Cowan, N.J.3
  • 29
    • 9644281539 scopus 로고    scopus 로고
    • Expression of a catalytically inactive transmembrane protein tyrosine phosphatase epsilon (tm-PTP epsilon) delays optic nerve myelination
    • Muja, N., G. Lovas, E. Romm, D. Machleder, M. Ranjan, V. Gallo, and L. D. Hudson. 2004. Expression of a catalytically inactive transmembrane protein tyrosine phosphatase epsilon (tm-PTP epsilon) delays optic nerve myelination. Glia 48:278-297.
    • (2004) Glia , vol.48 , pp. 278-297
    • Muja, N.1    Lovas, G.2    Romm, E.3    Machleder, D.4    Ranjan, M.5    Gallo, V.6    Hudson, L.D.7
  • 30
    • 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., N. Aoki, K. Aoyama, H. Shimizu, H. Shimano, N. Yamada, and H. Miyazaki. 2005. Receptor-type protein tyrosine phosphatase epsilon (PTPepsilonM) is a negative regulator of insulin signaling in primary hepatocytes and liver. Zool. Sci. 22:169-175.
    • (2005) Zool. 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
  • 31
    • 0030068389 scopus 로고    scopus 로고
    • Molecular cloning of a novel cytoplasmic protein tyrosine phosphatase PTP epsilon
    • Nakamura, K., Y. Mizuno, and K. Kikuchi. 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
  • 32
    • 0024801639 scopus 로고
    • The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau
    • Noble, M., S. A. Lewis, and N. J. Cowan. 1989. The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau. J. Cell Biol. 109:3367-3376.
    • (1989) J. Cell Biol , vol.109 , pp. 3367-3376
    • Noble, M.1    Lewis, S.A.2    Cowan, N.J.3
  • 33
    • 0034254725 scopus 로고    scopus 로고
    • Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon
    • Peretz, A., H. Gil-Henn, A. Sobko, V. Shinder, B. Attali, and A. Elson. 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
  • 34
    • 0030695246 scopus 로고    scopus 로고
    • Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit
    • Sapir, T., M. Elbaum, and O. Reiner. 1997. Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit. EMBO J. 16:6977-6984.
    • (1997) EMBO J , vol.16 , pp. 6977-6984
    • Sapir, T.1    Elbaum, M.2    Reiner, O.3
  • 36
    • 0033556074 scopus 로고    scopus 로고
    • Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation
    • Tanuma, N., K. Nakamura, and K. Kikuchi. 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
  • 37
    • 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., K. Nakamura, H. Shima, and K. Kikuchi. 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
  • 38
    • 0035892127 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin-10-induced JAK-STAT signaling
    • Tanuma, N., H. Shima, K. Nakamura, and K. Kikuchi. 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
  • 39
    • 0037468571 scopus 로고    scopus 로고
    • Reduced tumorigenicity of murine leukemia cells expressing protein-tyrosine phosphatase, PTPepsilon C
    • Tanuma, N., H. Shima, S. Shimada, and K. Kikuchi. 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
  • 40
    • 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., A. Peretz, B. Attali, and A. Elson. 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
  • 41
    • 33749485651 scopus 로고    scopus 로고
    • Tyrosine phosphatases epsilon and alpha perform specific and over-lapping functions in regulation of voltage-gated potassium channels in Schwann cells
    • Tiran, Z., A. Peretz, T. Sines, V. Shinder, J. Sap, B. Attali, and A. Elson. 2006. Tyrosine phosphatases epsilon and alpha perform specific and over-lapping functions in regulation of voltage-gated potassium channels in Schwann cells. Mol. Biol. Cell 17:4330-4342.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4330-4342
    • Tiran, Z.1    Peretz, A.2    Sines, T.3    Shinder, V.4    Sap, J.5    Attali, B.6    Elson, A.7
  • 44
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks, N. K. 2005. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121:667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 45
    • 0036065312 scopus 로고    scopus 로고
    • Expression of human protein tyrosine phosphatase epsilon in leucocytes: A potential ERK pathway-regulating phosphatase
    • Wabakken, T., H. Hauge, E. F. Finne, A. Wiedlocha, and H. Aasheim. 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
  • 46
    • 0028205103 scopus 로고
    • Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein
    • Wilkerson, C. G., S. M. King, and G. B. Witman. 1994. Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein. J. Cell Sci. 107:497-506.
    • (1994) J. Cell Sci , vol.107 , pp. 497-506
    • Wilkerson, C.G.1    King, S.M.2    Witman, G.B.3
  • 47
    • 21144445429 scopus 로고    scopus 로고
    • Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography
    • Zheng, H., P. Hu, D. F. Quinn, and Y. K. Wang. 2005. Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography. Mol. Cell Proteomics 4:721-730.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 721-730
    • Zheng, H.1    Hu, P.2    Quinn, D.F.3    Wang, Y.K.4
  • 48
    • 0037077275 scopus 로고    scopus 로고
    • Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation
    • Zheng, X. M., R. J. Resnick, and D. Shalloway. 2002. Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation. J. Biol. Chem. 277:21922-21929.
    • (2002) J. Biol. Chem , vol.277 , pp. 21922-21929
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 49
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng, X. M., R. J. Resnick, and D. Shalloway. 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
  • 50
    • 0035503358 scopus 로고    scopus 로고
    • Two mechanisms activate PTPalpha during mitosis
    • Zheng, X. M., and D. Shalloway. 2001. Two mechanisms activate PTPalpha during mitosis. EMBO J. 20:6037-6049.
    • (2001) EMBO J , vol.20 , pp. 6037-6049
    • Zheng, X.M.1    Shalloway, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.