메뉴 건너뛰기




Volumn 1833, Issue 5, 2013, Pages 1125-1132

Emerging role of tyrosine phosphatase, TCPTP, In the organelles of the early secretory pathway

Author keywords

Early secretory pathway; TCPTP; Tyrosine dephosphorylation; Tyrosine phosphatase TC48; Tyrosine phosphorylation; Vesicle trafficking

Indexed keywords

BCR ABL PROTEIN; CAVEOLIN 1; CLAUDIN; CYTOPLASM PROTEIN; ENDOPLASMIC RETICULUM GOLGI INTERMEDIATE COMPARTMENT PROTEIN 53; EPIDERMAL GROWTH FACTOR RECEPTOR; GAMMA INTERFERON; INTEGRIN; INTERLEUKIN 1; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MONENSIN; N ETHYLMALEIMIDE SENSITIVE FACTOR; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 2; NUCLEAR PROTEIN; PROTEIN TYROSINE PHOSPHATASE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; SYNTAXIN 17; TC45 PROTEIN; TC48 PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84874545993     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.01.004     Document Type: Article
Times cited : (18)

References (105)
  • 1
    • 0023651349 scopus 로고
    • A thousand and one protein kinases
    • Hunter T. A thousand and one protein kinases. Cell 1987, 50:823-829.
    • (1987) Cell , vol.50 , pp. 823-829
    • Hunter, T.1
  • 2
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 1995, 80:225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 3
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks N.K., Neel B.G. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell Biol. 2001, 13:182-195.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 5
    • 11244277091 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and the immune response
    • Mustelin T., Vang T., Bottini N. Protein tyrosine phosphatases and the immune response. Nat. Rev. Immunol. 2005, 5:43-57.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 43-57
    • Mustelin, T.1    Vang, T.2    Bottini, N.3
  • 7
    • 0035835824 scopus 로고    scopus 로고
    • PTEN: life as a tumor suppressor
    • Simpson L., Parsons R. PTEN: life as a tumor suppressor. Exp. Cell Res. 2001, 264:29-41.
    • (2001) Exp. Cell Res. , vol.264 , pp. 29-41
    • Simpson, L.1    Parsons, R.2
  • 8
    • 43049126784 scopus 로고    scopus 로고
    • PTP1B and TC-PTP: regulators of transformation and tumorigenesis
    • Stuible M., Doody K.M., Tremblay M.L. PTP1B and TC-PTP: regulators of transformation and tumorigenesis. Cancer Metastasis Rev. 2008, 27:215-230.
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 215-230
    • Stuible, M.1    Doody, K.M.2    Tremblay, M.L.3
  • 11
    • 0026510758 scopus 로고
    • Assignment of tyrosine-specific T-cell phosphatase to conserved syntenic groups on human chromosome 18 and mouse chromosome 18
    • Sakaguchi A.Y., Sylvia V.L., Martinez L., Smith E.A., Han E.S., Lalley P.A., Shows T.B., Choudhury G.G. Assignment of tyrosine-specific T-cell phosphatase to conserved syntenic groups on human chromosome 18 and mouse chromosome 18. Genomics 1992, 12:151-154.
    • (1992) Genomics , vol.12 , pp. 151-154
    • Sakaguchi, A.Y.1    Sylvia, V.L.2    Martinez, L.3    Smith, E.A.4    Han, E.S.5    Lalley, P.A.6    Shows, T.B.7    Choudhury, G.G.8
  • 12
    • 0026555257 scopus 로고
    • Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase
    • Mosinger B., Tillmann U., Westphal H., Tremblay M.L. Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:499-503.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 499-503
    • Mosinger, B.1    Tillmann, U.2    Westphal, H.3    Tremblay, M.L.4
  • 13
    • 0025902269 scopus 로고
    • Activation of transcription via AP-1 or CREB regulatory sites is blocked by protein tyrosine phosphatases
    • Champion-Arnaud P., Gesnel M.C., Foulkes N., Ronsin C., Sassone-Corsi P., Breathnach R. Activation of transcription via AP-1 or CREB regulatory sites is blocked by protein tyrosine phosphatases. Oncogene 1991, 6:1203-1209.
    • (1991) Oncogene , vol.6 , pp. 1203-1209
    • Champion-Arnaud, P.1    Gesnel, M.C.2    Foulkes, N.3    Ronsin, C.4    Sassone-Corsi, P.5    Breathnach, R.6
  • 14
    • 0026088990 scopus 로고
    • Molecular cloning and expression of a protein-tyrosine phosphatase showing homology with transcription factors Fos and Jun
    • Swarup G., Kamatkar S., Radha V., Rema V. Molecular cloning and expression of a protein-tyrosine phosphatase showing homology with transcription factors Fos and Jun. FEBS Lett. 1991, 280:65-69.
    • (1991) FEBS Lett. , vol.280 , pp. 65-69
    • Swarup, G.1    Kamatkar, S.2    Radha, V.3    Rema, V.4
  • 15
    • 0029563428 scopus 로고
    • Alternative splicing generates four different forms of a non-transmembrane protein tyrosine phosphatase mRNA
    • Reddy R.S., Swarup G. Alternative splicing generates four different forms of a non-transmembrane protein tyrosine phosphatase mRNA. DNA Cell Biol. 1995, 14:1007-1015.
    • (1995) DNA Cell Biol. , vol.14 , pp. 1007-1015
    • Reddy, R.S.1    Swarup, G.2
  • 16
    • 0028783629 scopus 로고
    • COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus
    • Lorenzen J.A., Dadabay C.Y., Fischer E.H. COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus. J. Cell Biol. 1995, 131:631-643.
    • (1995) J. Cell Biol. , vol.131 , pp. 631-643
    • Lorenzen, J.A.1    Dadabay, C.Y.2    Fischer, E.H.3
  • 17
    • 0028274296 scopus 로고
    • Nuclear localization and cell cycle regulation of a murine protein tyrosine phosphatase
    • Tillmann U., Wagner J., Boerboom D., Westphal H., Tremblay M.L. Nuclear localization and cell cycle regulation of a murine protein tyrosine phosphatase. Mol. Cell. Biol. 1994, 14:3030-3040.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3030-3040
    • Tillmann, U.1    Wagner, J.2    Boerboom, D.3    Westphal, H.4    Tremblay, M.L.5
  • 18
    • 0029998593 scopus 로고    scopus 로고
    • Two splice variants of a tyrosine phosphatase differ in substrate specificity, DNA binding, and subcellular location
    • Kamatkar S., Radha V., Nambirajan S., Reddy R.S., Swarup G. Two splice variants of a tyrosine phosphatase differ in substrate specificity, DNA binding, and subcellular location. J. Biol. Chem. 1996, 271:26755-26761.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26755-26761
    • Kamatkar, S.1    Radha, V.2    Nambirajan, S.3    Reddy, R.S.4    Swarup, G.5
  • 19
    • 0028316176 scopus 로고
    • Subcellular localization of a protein-tyrosine phosphatase: evidence for association with chromatin
    • Radha V., Nambirajan S., Swarup G. Subcellular localization of a protein-tyrosine phosphatase: evidence for association with chromatin. Biochem. J. 1994, 299(Pt 1):41-47.
    • (1994) Biochem. J. , vol.299 , Issue.PART 1 , pp. 41-47
    • Radha, V.1    Nambirajan, S.2    Swarup, G.3
  • 21
    • 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., Tiganis T. Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP. J. Biol. Chem. 2001, 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
  • 22
    • 0034058837 scopus 로고    scopus 로고
    • PTP-S2, a nuclear tyrosine phosphatase, is phosphorylated and excluded from condensed chromosomes during mitosis
    • Nambirajan S., Radha V., Kamatkar S., Swarup G. PTP-S2, a nuclear tyrosine phosphatase, is phosphorylated and excluded from condensed chromosomes during mitosis. J. Biosci. 2000, 25:33-40.
    • (2000) J. Biosci. , vol.25 , pp. 33-40
    • Nambirajan, S.1    Radha, V.2    Kamatkar, S.3    Swarup, G.4
  • 23
    • 0033600797 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling
    • Tiganis T., Kemp B.E., Tonks N.K. The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling. J. Biol. Chem. 1999, 274:27768-27775.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27768-27775
    • Tiganis, T.1    Kemp, B.E.2    Tonks, N.K.3
  • 25
    • 84872116942 scopus 로고    scopus 로고
    • Dynamic changes in nuclear localization of a DNA-binding protein tyrosine phosphatase TCPTP in response to DNA damage and replication arrest
    • Sree N.K., Anesh R., Radha V. Dynamic changes in nuclear localization of a DNA-binding protein tyrosine phosphatase TCPTP in response to DNA damage and replication arrest. Cell Biol. Toxicol. 2012, 28:409-419.
    • (2012) Cell Biol. Toxicol. , vol.28 , pp. 409-419
    • Sree, N.K.1    Anesh, R.2    Radha, V.3
  • 26
    • 78651070199 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase N2 regulates TNFalpha-induced signalling and cytokine secretion in human intestinal epithelial cells
    • Scharl M., McCole D.F., Weber A., Vavricka S.R., Frei P., Kellermeier S., Pesch T., Fried M., Rogler G. Protein tyrosine phosphatase N2 regulates TNFalpha-induced signalling and cytokine secretion in human intestinal epithelial cells. Gut 2011, 60:189-197.
    • (2011) Gut , vol.60 , pp. 189-197
    • Scharl, M.1    McCole, D.F.2    Weber, A.3    Vavricka, S.R.4    Frei, P.5    Kellermeier, S.6    Pesch, T.7    Fried, M.8    Rogler, G.9
  • 28
    • 33744530157 scopus 로고    scopus 로고
    • Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER
    • Gupta V., Swarup G. Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER. J. Cell Sci. 2006, 119:1703-1714.
    • (2006) J. Cell Sci. , vol.119 , pp. 1703-1714
    • Gupta, V.1    Swarup, G.2
  • 29
    • 0028236056 scopus 로고
    • Purification and crystallization of the catalytic domain of human protein tyrosine phosphatase 1B expressed in Escherichia coli
    • Barford D., Keller J.C., Flint A.J., Tonks N.K. Purification and crystallization of the catalytic domain of human protein tyrosine phosphatase 1B expressed in Escherichia coli. J. Mol. Biol. 1994, 239:726-730.
    • (1994) J. Mol. Biol. , vol.239 , pp. 726-730
    • Barford, D.1    Keller, J.C.2    Flint, A.J.3    Tonks, N.K.4
  • 31
    • 84874538233 scopus 로고    scopus 로고
    • PTP1B and TCPTP - nonredundant phosphatases in insulin signaling and glucose homeostasis
    • Tiganis T. PTP1B and TCPTP - nonredundant phosphatases in insulin signaling and glucose homeostasis. FEBS J. 2012.
    • (2012) FEBS J.
    • Tiganis, T.1
  • 32
    • 0039619868 scopus 로고    scopus 로고
    • Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on "substrate-trapping" mutants
    • Walchli S., Curchod M.L., Gobert R.P., Arkinstall S., Hooft van Huijsduijnen R. Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on "substrate-trapping" mutants. J. Biol. Chem. 2000, 275:9792-9796.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9792-9796
    • Walchli, S.1    Curchod, M.L.2    Gobert, R.P.3    Arkinstall, S.4    Hooft van Huijsduijnen, R.5
  • 33
    • 0031935043 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase
    • Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K. Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase. Mol. Cell. Biol. 1998, 18:1622-1634.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1622-1634
    • Tiganis, T.1    Bennett, A.M.2    Ravichandran, K.S.3    Tonks, N.K.4
  • 35
    • 33646868620 scopus 로고    scopus 로고
    • T-cell protein tyrosine phosphatase (Tcptp) is a negative regulator of colony-stimulating factor 1 signaling and macrophage differentiation
    • Simoncic P.D., Bourdeau A., Lee-Loy A., Rohrschneider L.R., Tremblay M.L., Stanley E.R., McGlade C.J. T-cell protein tyrosine phosphatase (Tcptp) is a negative regulator of colony-stimulating factor 1 signaling and macrophage differentiation. Mol. Cell. Biol. 2006, 26:4149-4160.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4149-4160
    • Simoncic, P.D.1    Bourdeau, A.2    Lee-Loy, A.3    Rohrschneider, L.R.4    Tremblay, M.L.5    Stanley, E.R.6    McGlade, C.J.7
  • 36
    • 59149103545 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase TCPTP controls VEGFR2 signalling
    • Mattila E., Auvinen K., Salmi M., Ivaska J. The protein tyrosine phosphatase TCPTP controls VEGFR2 signalling. J. Cell Sci. 2008, 121:3570-3580.
    • (2008) J. Cell Sci. , vol.121 , pp. 3570-3580
    • Mattila, E.1    Auvinen, K.2    Salmi, M.3    Ivaska, J.4
  • 37
    • 57749119550 scopus 로고    scopus 로고
    • Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase
    • Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M. Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase. J. Biol. Chem. 2008, 283:34374-34383.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34374-34383
    • Sangwan, V.1    Paliouras, G.N.2    Abella, J.V.3    Dube, N.4    Monast, A.5    Tremblay, M.L.6    Park, M.7
  • 38
    • 0036138705 scopus 로고    scopus 로고
    • A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus
    • Aoki N., Matsuda T. A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus. Mol. Endocrinol. 2002, 16:58-69.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 58-69
    • Aoki, N.1    Matsuda, T.2
  • 40
    • 0036033161 scopus 로고    scopus 로고
    • The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation
    • Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N., Matsuda T. The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation. Biochem. Biophys. Res. Commun. 2002, 297:811-817.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 811-817
    • Yamamoto, T.1    Sekine, Y.2    Kashima, K.3    Kubota, A.4    Sato, N.5    Aoki, N.6    Matsuda, T.7
  • 41
    • 33947221062 scopus 로고    scopus 로고
    • T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6
    • Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T., Lossos I.S. T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6. Mol. Cell. Biol. 2007, 27:2166-2179.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2166-2179
    • Lu, X.1    Chen, J.2    Sasmono, R.T.3    Hsi, E.D.4    Sarosiek, K.A.5    Tiganis, T.6    Lossos, I.S.7
  • 42
    • 0036006288 scopus 로고    scopus 로고
    • The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3
    • Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J. The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3. Curr. Biol. 2002, 12:446-453.
    • (2002) Curr. Biol. , vol.12 , pp. 446-453
    • Simoncic, P.D.1    Lee-Loy, A.2    Barber, D.L.3    Tremblay, M.L.4    McGlade, C.J.5
  • 43
    • 14944349510 scopus 로고    scopus 로고
    • Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase
    • van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J., Tremblay M.L., Tiganis T. Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase. Nat. Immunol. 2005, 6:253-260.
    • (2005) Nat. Immunol. , vol.6 , pp. 253-260
    • van Vliet, C.1    Bukczynska, P.E.2    Puryer, M.A.3    Sadek, C.M.4    Shields, B.J.5    Tremblay, M.L.6    Tiganis, T.7
  • 45
    • 78650058704 scopus 로고    scopus 로고
    • Integrin {alpha}1{beta}1 promotes caveolin-1 dephosphorylation by activating T cell protein-tyrosine phosphatase
    • Borza C.M., Chen X., Mathew S., Mont S., Sanders C.R., Zent R., Pozzi A. Integrin {alpha}1{beta}1 promotes caveolin-1 dephosphorylation by activating T cell protein-tyrosine phosphatase. J. Biol. Chem. 2010, 285:40114-40124.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40114-40124
    • Borza, C.M.1    Chen, X.2    Mathew, S.3    Mont, S.4    Sanders, C.R.5    Zent, R.6    Pozzi, A.7
  • 46
  • 47
    • 61849135255 scopus 로고    scopus 로고
    • T-cell protein tyrosine phosphatase is a key regulator in immune cell signaling: lessons from the knockout mouse model and implications in human disease
    • Doody K.M., Bourdeau A., Tremblay M.L. T-cell protein tyrosine phosphatase is a key regulator in immune cell signaling: lessons from the knockout mouse model and implications in human disease. Immunol. Rev. 2009, 228:325-341.
    • (2009) Immunol. Rev. , vol.228 , pp. 325-341
    • Doody, K.M.1    Bourdeau, A.2    Tremblay, M.L.3
  • 48
    • 29144492209 scopus 로고    scopus 로고
    • Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: from diabetes, obesity to cell cycle, and cancer
    • Dube N., Tremblay M.L. Involvement of the small protein tyrosine phosphatases TC-PTP and PTP1B in signal transduction and diseases: from diabetes, obesity to cell cycle, and cancer. Biochim. Biophys. Acta 2005, 1754:108-117.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 108-117
    • Dube, N.1    Tremblay, M.L.2
  • 50
    • 67249132591 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases PTP-1B and TC-PTP play nonredundant roles in macrophage development and IFN-gamma signaling
    • Heinonen K.M., Bourdeau A., Doody K.M., Tremblay M.L. Protein tyrosine phosphatases PTP-1B and TC-PTP play nonredundant roles in macrophage development and IFN-gamma signaling. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9368-9372.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9368-9372
    • Heinonen, K.M.1    Bourdeau, A.2    Doody, K.M.3    Tremblay, M.L.4
  • 52
    • 84969213492 scopus 로고    scopus 로고
    • Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls
    • Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls. Nature 2007, 447:661-678.
    • (2007) Nature , vol.447 , pp. 661-678
  • 56
    • 57649166494 scopus 로고    scopus 로고
    • Eating the enemy within: autophagy in infectious diseases
    • Orvedahl A., Levine B. Eating the enemy within: autophagy in infectious diseases. Cell Death Differ. 2009, 16:57-69.
    • (2009) Cell Death Differ. , vol.16 , pp. 57-69
    • Orvedahl, A.1    Levine, B.2
  • 59
    • 84861994381 scopus 로고    scopus 로고
    • The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation
    • Scharl M., Rogler G. The role for protein tyrosine phosphatase nonreceptor type 2 in regulating autophagosome formation. Ann. N. Y. Acad. Sci. 2012, 1257:93-102.
    • (2012) Ann. N. Y. Acad. Sci. , vol.1257 , pp. 93-102
    • Scharl, M.1    Rogler, G.2
  • 61
    • 77957358053 scopus 로고    scopus 로고
    • Loss of protein tyrosine phosphatase N2 potentiates epidermal growth factor suppression of intestinal epithelial chloride secretion
    • Scharl M., Rudenko I., McCole D.F. Loss of protein tyrosine phosphatase N2 potentiates epidermal growth factor suppression of intestinal epithelial chloride secretion. Am. J. Physiol. Gastrointest. Liver Physiol. 2010, 299:G935-G945.
    • (2010) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.299
    • Scharl, M.1    Rudenko, I.2    McCole, D.F.3
  • 62
    • 78649605952 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase non-receptor Type 2 regulates IFN-gamma-induced cytokine signaling in THP-1 monocytes
    • Scharl M., Hruz P., McCole D.F. Protein tyrosine phosphatase non-receptor Type 2 regulates IFN-gamma-induced cytokine signaling in THP-1 monocytes. Inflamm. Bowel Dis. 2010, 16:2055-2064.
    • (2010) Inflamm. Bowel Dis. , vol.16 , pp. 2055-2064
    • Scharl, M.1    Hruz, P.2    McCole, D.F.3
  • 63
    • 12344285901 scopus 로고    scopus 로고
    • Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP
    • Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J. Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP. Nat. Cell Biol. 2005, 7:78-85.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 78-85
    • Mattila, E.1    Pellinen, T.2    Nevo, J.3    Vuoriluoto, K.4    Arjonen, A.5    Ivaska, J.6
  • 64
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1-dependent beta1 integrin endocytosis is a critical regulator of fibronectin turnover
    • Shi F., Sottile J. Caveolin-1-dependent beta1 integrin endocytosis is a critical regulator of fibronectin turnover. J. Cell Sci. 2008, 121:2360-2371.
    • (2008) J. Cell Sci. , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 65
    • 56249093843 scopus 로고    scopus 로고
    • Caveolin-1, transforming growth factor-beta receptor internalization, and the pathogenesis of systemic sclerosis
    • Del Galdo F., Lisanti M.P., Jimenez S.A. Caveolin-1, transforming growth factor-beta receptor internalization, and the pathogenesis of systemic sclerosis. Curr. Opin. Rheumatol. 2008, 20:713-719.
    • (2008) Curr. Opin. Rheumatol. , vol.20 , pp. 713-719
    • Del Galdo, F.1    Lisanti, M.P.2    Jimenez, S.A.3
  • 67
    • 1542289711 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-mediated signal transduction from endosomes
    • Wang Y., Pennock S.D., Chen X., Kazlauskas A., Wang Z. Platelet-derived growth factor receptor-mediated signal transduction from endosomes. J. Biol. Chem. 2004, 279:8038-8046.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8038-8046
    • Wang, Y.1    Pennock, S.D.2    Chen, X.3    Kazlauskas, A.4    Wang, Z.5
  • 68
    • 33750509827 scopus 로고    scopus 로고
    • Loss of T-cell protein tyrosine phosphatase induces recycling of the platelet-derived growth factor (PDGF) beta-receptor but not the PDGF alpha-receptor
    • Karlsson S., Kowanetz K., Sandin A., Persson C., Ostman A., Heldin C.H., Hellberg C. Loss of T-cell protein tyrosine phosphatase induces recycling of the platelet-derived growth factor (PDGF) beta-receptor but not the PDGF alpha-receptor. Mol. Biol. Cell 2006, 17:4846-4855.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4846-4855
    • Karlsson, S.1    Kowanetz, K.2    Sandin, A.3    Persson, C.4    Ostman, A.5    Heldin, C.H.6    Hellberg, C.7
  • 69
    • 0028927012 scopus 로고
    • Altered subcellular location of an activated and tumour-associated epidermal growth factor receptor
    • Ekstrand A.J., Liu L., He J., Hamid M.L., Longo N., Collins V.P., James C.D. Altered subcellular location of an activated and tumour-associated epidermal growth factor receptor. Oncogene 1995, 10:1455-1460.
    • (1995) Oncogene , vol.10 , pp. 1455-1460
    • Ekstrand, A.J.1    Liu, L.2    He, J.3    Hamid, M.L.4    Longo, N.5    Collins, V.P.6    James, C.D.7
  • 70
    • 3543041878 scopus 로고    scopus 로고
    • Defective downregulation of receptor tyrosine kinases in cancer
    • Bache K.G., Slagsvold T., Stenmark H. Defective downregulation of receptor tyrosine kinases in cancer. EMBO J. 2004, 23:2707-2712.
    • (2004) EMBO J. , vol.23 , pp. 2707-2712
    • Bache, K.G.1    Slagsvold, T.2    Stenmark, H.3
  • 71
    • 80051840811 scopus 로고    scopus 로고
    • TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells
    • Mitra A., Kalayarasan S., Gupta V., Radha V. TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells. PLoS One 2011, 6:e23681.
    • (2011) PLoS One , vol.6
    • Mitra, A.1    Kalayarasan, S.2    Gupta, V.3    Radha, V.4
  • 72
    • 79960113049 scopus 로고    scopus 로고
    • Signalling to actin: role of C3G, a multitasking guanine-nucleotide-exchange factor
    • Radha V., Mitra A., Dayma K., Sasikumar K. Signalling to actin: role of C3G, a multitasking guanine-nucleotide-exchange factor. Biosci. Rep. 2011, 31:231-244.
    • (2011) Biosci. Rep. , vol.31 , pp. 231-244
    • Radha, V.1    Mitra, A.2    Dayma, K.3    Sasikumar, K.4
  • 73
    • 84867205163 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway
    • Muppirala M., Gupta V., Swarup G. Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway. Biochim. Biophys. Acta 2012, 1823:2109-2119.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 2109-2119
    • Muppirala, M.1    Gupta, V.2    Swarup, G.3
  • 74
    • 84869101198 scopus 로고    scopus 로고
    • The tyrosine phosphatase TC48 interacts with and inactivates the oncogenic fusion protein BCR-Abl but not cellular Abl
    • Mitra A., Sasikumar K., Parthasaradhi B.V., Radha V. The tyrosine phosphatase TC48 interacts with and inactivates the oncogenic fusion protein BCR-Abl but not cellular Abl. Biochim. Biophys. Acta 2013, 1832:275-284.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 275-284
    • Mitra, A.1    Sasikumar, K.2    Parthasaradhi, B.V.3    Radha, V.4
  • 75
    • 70149084008 scopus 로고    scopus 로고
    • The p24 family and selective transport processes at the ER-Golgi interface
    • Strating J.R., Martens G.J. The p24 family and selective transport processes at the ER-Golgi interface. Biol. Cell 2009, 101:495-509.
    • (2009) Biol. Cell , vol.101 , pp. 495-509
    • Strating, J.R.1    Martens, G.J.2
  • 76
    • 10444288648 scopus 로고    scopus 로고
    • Phosphorylated guanine nucleotide exchange factor C3G, induced by pervanadate and Src family kinases localizes to the Golgi and subcortical actin cytoskeleton
    • Radha V., Rajanna A., Swarup G. Phosphorylated guanine nucleotide exchange factor C3G, induced by pervanadate and Src family kinases localizes to the Golgi and subcortical actin cytoskeleton. BMC Cell Biol. 2004, 5:31.
    • (2004) BMC Cell Biol. , vol.5 , pp. 31
    • Radha, V.1    Rajanna, A.2    Swarup, G.3
  • 77
    • 79959340062 scopus 로고    scopus 로고
    • Syntaxin 17cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi
    • Muppirala M., Gupta V., Swarup G. Syntaxin 17cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi. Biol. Cell 2011, 103:333-350.
    • (2011) Biol. Cell , vol.103 , pp. 333-350
    • Muppirala, M.1    Gupta, V.2    Swarup, G.3
  • 78
    • 0033840553 scopus 로고    scopus 로고
    • Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics
    • Steegmaier M., Oorschot V., Klumperman J., Scheller R.H. Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics. Mol. Biol. Cell 2000, 11:2719-2731.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2719-2731
    • Steegmaier, M.1    Oorschot, V.2    Klumperman, J.3    Scheller, R.H.4
  • 80
    • 0035976927 scopus 로고    scopus 로고
    • Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin
    • Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J. Biol. Chem. 2001, 276:45298-45306.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45298-45306
    • Sohda, M.1    Misumi, Y.2    Yamamoto, A.3    Yano, A.4    Nakamura, N.5    Ikehara, Y.6
  • 82
    • 78650010073 scopus 로고    scopus 로고
    • Reticulon short hairpin transmembrane domains are used to shape ER tubules
    • Zurek N., Sparks L., Voeltz G. Reticulon short hairpin transmembrane domains are used to shape ER tubules. Traffic 2011, 12:28-41.
    • (2011) Traffic , vol.12 , pp. 28-41
    • Zurek, N.1    Sparks, L.2    Voeltz, G.3
  • 84
    • 0037119364 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum
    • Wyles J.P., McMaster C.R., Ridgway N.D. Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. J. Biol. Chem. 2002, 277:29908-29918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29908-29918
    • Wyles, J.P.1    McMaster, C.R.2    Ridgway, N.D.3
  • 85
    • 0141867737 scopus 로고    scopus 로고
    • PECAM-1: old friend, new partners
    • Ilan N., Madri J.A. PECAM-1: old friend, new partners. Curr. Opin. Cell Biol. 2003, 15:515-524.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 515-524
    • Ilan, N.1    Madri, J.A.2
  • 86
    • 0028301657 scopus 로고
    • Tyrosine phosphorylation of P-selectin in intact platelets and in a disulphide-linked complex with immunoprecipitated pp 60c-src
    • Modderman P.W., von dem Borne A.E., Sonnenberg A. Tyrosine phosphorylation of P-selectin in intact platelets and in a disulphide-linked complex with immunoprecipitated pp 60c-src. Biochem. J. 1994, 299(Pt 3):613-621.
    • (1994) Biochem. J. , vol.299 , Issue.PART 3 , pp. 613-621
    • Modderman, P.W.1    von dem Borne, A.E.2    Sonnenberg, A.3
  • 87
    • 0038120892 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology
    • Newman P.J., Newman D.K. Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology. Arterioscler. Thromb. Vasc. Biol. 2003, 23:953-964.
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , pp. 953-964
    • Newman, P.J.1    Newman, D.K.2
  • 88
    • 0028358876 scopus 로고
    • CD31 (PECAM-1), CDw32 (Fc gamma RII), and anti-HLA class I monoclonal antibodies recognize phosphotyrosine-containing proteins on the surface of human neutrophils
    • Skubitz K.M., Goueli S.A. CD31 (PECAM-1), CDw32 (Fc gamma RII), and anti-HLA class I monoclonal antibodies recognize phosphotyrosine-containing proteins on the surface of human neutrophils. J. Immunol. 1994, 152:5902-5911.
    • (1994) J. Immunol. , vol.152 , pp. 5902-5911
    • Skubitz, K.M.1    Goueli, S.A.2
  • 90
    • 66949112599 scopus 로고    scopus 로고
    • Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion
    • Tomihari M., Hwang S.H., Chung J.S., Cruz P.D., Ariizumi K. Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion. Exp. Dermatol. 2009, 18:586-595.
    • (2009) Exp. Dermatol. , vol.18 , pp. 586-595
    • Tomihari, M.1    Hwang, S.H.2    Chung, J.S.3    Cruz, P.D.4    Ariizumi, K.5
  • 92
    • 74049162940 scopus 로고    scopus 로고
    • RTN3 inducing apoptosis is modulated by an adhesion protein CRELD1
    • Xiang R., Zhao S. RTN3 inducing apoptosis is modulated by an adhesion protein CRELD1. Mol. Cell. Biochem. 2009, 331:225-230.
    • (2009) Mol. Cell. Biochem. , vol.331 , pp. 225-230
    • Xiang, R.1    Zhao, S.2
  • 94
    • 0141644213 scopus 로고    scopus 로고
    • The JAM family of junctional adhesion molecules
    • Bazzoni G. The JAM family of junctional adhesion molecules. Curr. Opin. Cell Biol. 2003, 15:525-530.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 525-530
    • Bazzoni, G.1
  • 95
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim. Biophys. Acta 2005, 1744:493-517.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 98
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature 1994, 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 100
    • 77955238543 scopus 로고    scopus 로고
    • A targeted siRNA screen to identify SNAREs required for constitutive secretion in mammalian cells
    • Gordon D.E., Bond L.M., Sahlender D.A., Peden A.A. A targeted siRNA screen to identify SNAREs required for constitutive secretion in mammalian cells. Traffic 2010, 11:1191-1204.
    • (2010) Traffic , vol.11 , pp. 1191-1204
    • Gordon, D.E.1    Bond, L.M.2    Sahlender, D.A.3    Peden, A.A.4
  • 101
    • 1842424803 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-1B dephosphorylation of the insulin receptor occurs in a perinuclear endosome compartment in human embryonic kidney 293 cells
    • Romsicki Y., Reece M., Gauthier J.Y., Asante-Appiah E., Kennedy B.P. Protein tyrosine phosphatase-1B dephosphorylation of the insulin receptor occurs in a perinuclear endosome compartment in human embryonic kidney 293 cells. J. Biol. Chem. 2004, 279:12868-12875.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12868-12875
    • Romsicki, Y.1    Reece, M.2    Gauthier, J.Y.3    Asante-Appiah, E.4    Kennedy, B.P.5
  • 102
    • 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., Bastiaens P.I. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 2002, 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
  • 103
    • 78049253878 scopus 로고    scopus 로고
    • In control at the ER: PTP1B and the down-regulation of RTKs by dephosphorylation and endocytosis
    • Stuible M., Tremblay M.L. In control at the ER: PTP1B and the down-regulation of RTKs by dephosphorylation and endocytosis. Trends Cell Biol. 2010, 20:672-679.
    • (2010) Trends Cell Biol. , vol.20 , pp. 672-679
    • Stuible, M.1    Tremblay, M.L.2
  • 104
    • 84455169839 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B modulates early endosome fusion and trafficking of Met and epidermal growth factor receptors
    • Sangwan V., Abella J., Lai A., Bertos N., Stuible M., Tremblay M.L., Park M. Protein-tyrosine phosphatase 1B modulates early endosome fusion and trafficking of Met and epidermal growth factor receptors. J. Biol. Chem. 2011, 286:45000-45013.
    • (2011) J. Biol. Chem. , vol.286 , pp. 45000-45013
    • Sangwan, V.1    Abella, J.2    Lai, A.3    Bertos, N.4    Stuible, M.5    Tremblay, M.L.6    Park, M.7
  • 105
    • 67449095681 scopus 로고    scopus 로고
    • PTP1B dephosphorylates N-ethylmaleimide-sensitive factor and elicits SNARE complex disassembly during human sperm exocytosis
    • Zarelli V.E., Ruete M.C., Roggero C.M., Mayorga L.S., Tomes C.N. PTP1B dephosphorylates N-ethylmaleimide-sensitive factor and elicits SNARE complex disassembly during human sperm exocytosis. J. Biol. Chem. 2009, 284:10491-10503.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10491-10503
    • Zarelli, V.E.1    Ruete, M.C.2    Roggero, C.M.3    Mayorga, L.S.4    Tomes, C.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.