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Volumn 287, Issue 25, 2012, Pages 20942-20956

Striatal-enriched protein-tyrosine phosphatase (STEP) regulates Pyk2 kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETAL; DEPHOSPHORYLATES; FOCAL ADHESION KINASE; HEMATOPOIETIC CELL; KINASE ACTIVITY; LONG-TERM POTENTIATIONS; N METHYL D ASPARTATE RECEPTOR; PAXILLIN; POSTSYNAPTIC DENSITIES; PROLINE-RICH TYROSINE KINASE 2; PROTEIN-TYROSINE PHOSPHATASE; SRC FAMILY; SYNAPTIC MEMBRANES; TYROSINE KINASE;

EID: 84862296991     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.368654     Document Type: Article
Times cited : (69)

References (68)
  • 2
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase β, a novel protein tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki, H., Nagura, K., Ishino, M., Tobioka, H., Kotani, K., and Sasaki, T. (1995) Cloning and characterization of cell adhesion kinase β, a novel protein tyrosine kinase of the focal adhesion kinase subfamily. J. Biol. Chem. 270, 21206-21219
    • (1995) J. Biol. Chem. , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 3
    • 0032590021 scopus 로고    scopus 로고
    • +and PYK2/CAKβ, two related tyrosine kinases highly expressed in the central nervous system: Similarities and differences in the expression pattern
    • + and PYK2/CAKβ, two related tyrosine kinases highly expressed in the central nervous system: similarities and differences in the expression pattern. Eur. J. Neurosci. 11, 3777-3788
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 3777-3788
    • Menegon, A.1    Burgaya, F.2    Baudot, P.3    Dunlap, D.D.4    Girault, J.A.5    Valtorta, F.6
  • 4
    • 0032586727 scopus 로고    scopus 로고
    • FAK and PYK2/CAKβ in the nervous system: A link between neuronal activity, plasticity and survival?
    • DOI 10.1016/S0166-2236(98)01358-7, PII S0166223698013587
    • Girault, J. A., Costa, A., Derkinderen, P., Studler, J. M., and Toutant, M. (1999) FAK and PYK2/CAKβ in the nervous system: a link between neuronal activity, plasticity and survival? Trends Neurosci. 22, 257-263 (Pubitemid 29259992)
    • (1999) Trends in Neurosciences , vol.22 , Issue.6 , pp. 257-263
    • Girault, J.-A.1    Costa, A.2    Derkinderen, P.3    Studler, J.-M.4    Toutant, M.5
  • 5
    • 41249100434 scopus 로고    scopus 로고
    • Calcium-dependent Pyk2 activation: A role for calmodulin?
    • Schaller, M. D. (2008) Calcium-dependent Pyk2 activation: a role for calmodulin? Biochem. J. 410, e3-e4
    • (2008) Biochem. J. , vol.410
    • Schaller, M.D.1
  • 7
    • 0031814171 scopus 로고    scopus 로고
    • +and PYK2/Cakß, two related tyrosine kinases, in rat hippocampal slices: Effects of LPA, carbachol, depolarization and hyperosmolarity
    • + and PYK2/Cakß, two related tyrosine kinases, in rat hippocampal slices: effects of LPA, carbachol, depolarization and hyperosmolarity. Eur. J. Neurosci. 10, 1667-1675
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1667-1675
    • Derkinderen, P.1    Siciliano, J.2    Toutant, M.3    Girault, J.A.4
  • 8
    • 0032547831 scopus 로고    scopus 로고
    • Calcium- and protein kinase C-dependent activation of the tyrosine kinase PYK2 by angiotensin II in vascular smooth muscle
    • Sabri, A., Govindarajan, G., Griffin, T. M., Byron, K. L., Samarel, A. M., and Lucchesi, P. A. (1998) Calcium- and protein kinase C-dependent activation of the tyrosine kinase PYK2 by angiotensin II in vascular smooth muscle. Circ. Res. 83, 841-851 (Pubitemid 28489081)
    • (1998) Circulation Research , vol.83 , Issue.8 , pp. 841-851
    • Sabri, A.1    Govindarajan, G.2    Griffin, T.M.3    Byron, K.L.4    Samarel, A.M.5    Lucchesi, P.A.6
  • 9
    • 0034659716 scopus 로고    scopus 로고
    • In CA1 pyramidal neurons of the hippocampus protein kinase C regulates calcium-dependent inactivation of NMDA receptors
    • Lu, W. Y., Jackson, M. F., Bai, D., Orser, B. A., and MacDonald, J. F. (2000) In CA1 pyramidal neurons of the hippocampus protein kinase C regulates calcium dependent inactivation of NMDA receptors. J. Neurosci. 20, 4452-4461 (Pubitemid 30396610)
    • (2000) Journal of Neuroscience , vol.20 , Issue.12 , pp. 4452-4461
    • Lu, W.-Y.1    Jackson, M.F.2    Bai, D.3    Orser, B.A.4    MacDonald, J.F.5
  • 12
    • 55549135364 scopus 로고    scopus 로고
    • The transactivated epidermal growth factor receptor recruits Pyk2 to regulate Src kinase activity
    • Schauwienold, D., Sastre, A. P., Genzel, N., Schaefer, M., and Reusch, H. P. (2008) The transactivated epidermal growth factor receptor recruits Pyk2 to regulate Src kinase activity. J. Biol. Chem. 283, 27748-27756
    • (2008) J. Biol. Chem. , vol.283 , pp. 27748-27756
    • Schauwienold, D.1    Sastre, A.P.2    Genzel, N.3    Schaefer, M.4    Reusch, H.P.5
  • 13
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • DOI 10.1038/383547a0
    • Dikic, I., Tokiwa, G., Lev, S., Courtneidge, S. A., and Schlessinger, J. (1996) A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383, 547-550 (Pubitemid 26346184)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 14
    • 4043054389 scopus 로고    scopus 로고
    • RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner
    • DOI 10.1074/jbc.M313527200
    • Park, S. Y., Avraham, H. K., and Avraham, S. (2004) RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner. J. Biol. Chem. 279, 33315-33322 (Pubitemid 39062979)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33315-33322
    • Park, S.-Y.1    Avraham, H.K.2    Avraham, S.3
  • 16
    • 0033591228 scopus 로고    scopus 로고
    • Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades
    • Blaukat, A., Ivankovic-Dikic, I., Grönroos, E., Dolfi, F., Tokiwa, G., Vuori, K., and Dikic, I. (1999) Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades. J. Biol. Chem. 274, 14893-14901
    • (1999) J. Biol. Chem. , vol.274 , pp. 14893-14901
    • Blaukat, A.1    Ivankovic-Dikic, I.2    Grönroos, E.3    Dolfi, F.4    Tokiwa, G.5    Vuori, K.6    Dikic, I.7
  • 18
    • 1842731881 scopus 로고    scopus 로고
    • SRC kinases: A hub for NMDA receptor regulation
    • Salter, M. W., and Kalia, L. V. (2004) Src kinases: a hub for NMDA receptor regulation. Nat. Rev. Neurosci. 5, 317-328 (Pubitemid 38478658)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.4 , pp. 317-328
    • Salter, M.W.1    Kalia, L.V.2
  • 19
    • 0032718010 scopus 로고    scopus 로고
    • Negative regulation of PYK2/related adhesion focal tyrosine kinase signal transduction by hematopoietic tyrosine phosphatase SHPTP1
    • Kumar, S., Avraham, S., Bharti, A., Goyal, J., Pandey, P., and Kharbanda, S. (1999) Negative regulation of PYK2/related adhesion focal tyrosine kinase signal transduction by hematopoietic tyrosine phosphatase SHPTP1. J. Biol. Chem. 274, 30657-30663
    • (1999) J. Biol. Chem. , vol.274 , pp. 30657-30663
    • Kumar, S.1    Avraham, S.2    Bharti, A.3    Goyal, J.4    Pandey, P.5    Kharbanda, S.6
  • 20
    • 0035968322 scopus 로고    scopus 로고
    • Inhibition of the catalytic activity of cell adhesion kinase β by proteintyrosine phosphatase-PEST-mediated dephosphorylation
    • Lyons, P. D., Dunty, J. M., Schaefer, E. M., and Schaller, M. D. (2001) Inhibition of the catalytic activity of cell adhesion kinase β by proteintyrosine phosphatase-PEST-mediated dephosphorylation. J. Biol. Chem. 276, 24422-24431
    • (2001) J. Biol. Chem. , vol.276 , pp. 24422-24431
    • Lyons, P.D.1    Dunty, J.M.2    Schaefer, E.M.3    Schaller, M.D.4
  • 21
    • 19544390842 scopus 로고    scopus 로고
    • Interferon-γ-dependent tyrosine phosphorylation of MEKK4 via Pyk2 is regulated by annexin II and SHP2 in keratinocytes
    • DOI 10.1042/BJ20041236
    • Halfter, U. M., Derbyshire, Z. E., and Vaillancourt, R. R. (2005) Interferon-γ-dependent tyrosine phosphorylation of MEKK4 via Pyk2 is regulated by annexin II and SHP2 in keratinocytes. Biochem. J. 388, 17-28 (Pubitemid 40732928)
    • (2005) Biochemical Journal , vol.388 , Issue.1 , pp. 17-28
    • Halfter, U.M.1    Derbyshire, Z.E.2    Vaillancourt, R.R.3
  • 22
    • 0035796465 scopus 로고    scopus 로고
    • PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates
    • DOI 10.1093/emboj/20.13.3414
    • Davidson, D., and Veillette, A. (2001) PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates. EMBO J. 20, 3414-3426 (Pubitemid 32634349)
    • (2001) EMBO Journal , vol.20 , Issue.13 , pp. 3414-3426
    • Davidson, D.1    Veillette, A.2
  • 23
    • 0037220735 scopus 로고    scopus 로고
    • NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling
    • DOI 10.1038/nn989
    • Paul, S., Nairn, A. C., Wang, P., and Lombroso, P. J. (2003) NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling. Nat. Neurosci. 6, 34-42 (Pubitemid 36026330)
    • (2003) Nature Neuroscience , vol.6 , Issue.1 , pp. 34-42
    • Paul, S.1    Nairn, A.C.2    Wang, P.3    Lombroso, P.J.4
  • 24
    • 0037954344 scopus 로고    scopus 로고
    • Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38α is determined by a kinase specificity sequence and influenced by reducing agents
    • DOI 10.1042/BJ20021941
    • Muñoz, J. J., Tárrega, C., Blanco-Aparicio, C., and Pulido, R. (2003) Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38α is determined by a kinase specificity sequence and influenced by reducing agents. Biochem. J. 372, 193-201 (Pubitemid 36609621)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 193-201
    • Munoz, J.J.1    Tarrega, C.2    Blanco-Aparicio, C.3    Pulido, R.4
  • 25
    • 0037025303 scopus 로고    scopus 로고
    • Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420
    • DOI 10.1074/jbc.M111683200
    • Nguyen, T. H., Liu, J., and Lombroso, P. J. (2002) Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420. J. Biol. Chem. 277, 24274-24279 (Pubitemid 34951945)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24274-24279
    • Nguyen, T.-H.1    Liu, J.2    Lombroso, P.J.3
  • 29
    • 59449110909 scopus 로고    scopus 로고
    • DOG 1.0: Illustrator of protein domain structures
    • Ren, J., Wen, L., Gao, X., Jin, C., Xue, Y., and Yao, X. (2009) DOG 1.0: illustrator of protein domain structures. Cell Res. 19, 271-273
    • (2009) Cell Res. , vol.19 , pp. 271-273
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 31
    • 60349088785 scopus 로고    scopus 로고
    • Phospho-regulation of synaptic and extrasynaptic N-methyl-D-aspartate receptors in adult hippocampal slices
    • Goebel-Goody, S. M., Davies, K. D., Alvestad Linger, R. M., Freund, R. K., and Browning, M. D. (2009) Phospho-regulation of synaptic and extrasynaptic N-methyl-D-aspartate receptors in adult hippocampal slices. Neuroscience 158, 1446-1459
    • (2009) Neuroscience , vol.158 , pp. 1446-1459
    • Goebel-Goody, S.M.1    Davies, K.D.2    Alvestad Linger, R.M.3    Freund, R.K.4    Browning, M.D.5
  • 32
    • 0037077301 scopus 로고    scopus 로고
    • Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102
    • DOI 10.1074/jbc.M112339200
    • Lim, I. A., Hall, D. D., and Hell, J. W. (2002) Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102. J. Biol. Chem. 277, 21697-21711 (Pubitemid 34952321)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21697-21711
    • Lim, I.A.1    Hall, D.D.2    Hell, J.W.3
  • 33
    • 0030902281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling
    • DOI 10.1084/jem.185.7.1253
    • Qian, D., Lev, S., van Oers, N. S., Dikic, I., Schlessinger, J., and Weiss, A. (1997) Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling. J. Exp. Med. 185, 1253-1259 (Pubitemid 27172906)
    • (1997) Journal of Experimental Medicine , vol.185 , Issue.7 , pp. 1253-1259
    • Qian, D.1    Lev, S.2    Van Oers, N.S.C.3    Dikic, I.4    Schlessinger, J.5    Weiss, A.6
  • 34
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • DOI 10.1093/emboj/18.9.2459
    • Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A., and Soriano, P. (1999) Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459-2471 (Pubitemid 29213279)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 35
    • 47249118481 scopus 로고    scopus 로고
    • Noonan syndrome-associated SHP-2/Ptpn11 mutants enhance SIRPα and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation
    • Eminaga, S., and Bennett, A. M. (2008) Noonan syndrome-associated SHP-2/Ptpn11 mutants enhance SIRPα and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation. J. Biol. Chem. 283, 15328-15338
    • (2008) J. Biol. Chem. , vol.283 , pp. 15328-15338
    • Eminaga, S.1    Bennett, A.M.2
  • 36
    • 0032534791 scopus 로고    scopus 로고
    • PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
    • DOI 10.1093/emboj/17.24.7337
    • Pulido, R., Zúñiga, A., and Ullrich, A. (1998) PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J. 17, 7337-7350 (Pubitemid 29002702)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7337-7350
    • Pulido, R.1    Zuniga, A.2    Ullrich, A.3
  • 37
    • 0032489362 scopus 로고    scopus 로고
    • Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells
    • DOI 10.1074/jbc.273.10.5692
    • Ostergaard, H. L., Lou, O., Arendt, C. W., and Berg, N. N. (1998) Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells. J. Biol. Chem. 273, 5692-5696 (Pubitemid 28124041)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5692-5696
    • Ostergaard, H.L.1    Lou, O.2    Arendt, C.W.3    Berg, N.N.4
  • 39
    • 0042031108 scopus 로고    scopus 로고
    • The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1
    • DOI 10.1074/jbc.M302278200
    • Kruljac-Letunic, A., Moelleken, J., Kallin, A., Wieland, F., and Blaukat, A. (2003) The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1. J. Biol. Chem. 278, 29560-29570 (Pubitemid 36962338)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29560-29570
    • Kruljac-Letunic, A.1    Moelleken, J.2    Kallin, A.3    Wieland, F.4    Blaukat, A.5
  • 40
    • 12844275929 scopus 로고    scopus 로고
    • Depolarization activates ERK and proline-rich tyrosine kinase 2 (PYK2) independently in different cellular compartments in hippocampal slices
    • DOI 10.1074/jbc.M411312200
    • Corvol, J. C., Valjent, E., Toutant, M., Enslen, H., Irinopoulou, T., Lev, S., Hervé, D., and Girault, J. A. (2005) Depolarization activates ERK and proline-rich tyrosine kinase 2 (PYK2) independently in different cellular compartments in hippocampal slices. J. Biol. Chem. 280, 660-668 (Pubitemid 40165033)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 660-668
    • Corvol, J.-C.1    Valjent, E.2    Toutant, M.3    Enslen, H.4    Irinopoulou, T.5    Lev, S.6    Herve, D.7    Girault, J.-A.8
  • 41
    • 0034237577 scopus 로고    scopus 로고
    • Protein transduction: Unrestricted delivery into all cells?
    • DOI 10.1016/S0962-8924(00)01771-2, PII S0962892400017712
    • Schwarze, S. R., Hruska, K. A., and Dowdy, S. F. (2000) Protein transduction: unrestricted delivery into all cells? Trends. Cell Biol. 10, 290-295 (Pubitemid 30387038)
    • (2000) Trends in Cell Biology , vol.10 , Issue.7 , pp. 290-295
    • Schwarze, S.R.1    Hruska, K.A.2    Dowdy, S.F.3
  • 42
    • 33749531024 scopus 로고    scopus 로고
    • Rapid isolation of synaptoneurosomes and postsynaptic densities from adult mouse hippocampus
    • DOI 10.1016/j.jneumeth.2006.05.008, PII S016502700600238X
    • Villasana, L. E., Klann, E., and Tejada-Simon, M. V. (2006) Rapid isolation of synaptoneurosomes and postsynaptic densities from adult mouse hippocampus. J. Neurosci. Methods 158, 30-36 (Pubitemid 44528760)
    • (2006) Journal of Neuroscience Methods , vol.158 , Issue.1 , pp. 30-36
    • Villasana, L.E.1    Klann, E.2    Tejada-Simon, M.V.3
  • 43
    • 0034255148 scopus 로고    scopus 로고
    • The dopamine/D1 receptor mediates the phosphorylation and inactivation of the protein tyrosine phosphatase STEP via a PKA-dependent pathway
    • Paul, S., Snyder, G. L., Yokakura, H., Picciotto, M. R., Nairn, A. C., and Lombroso, P. J. (2000) Dopamine/D1 receptor mediates the phosphorylation and inactivation of the protein tyrosine phosphatase, STEP, through a PKA-mediated pathway. J. Neurosci. 20, 5630-5638 (Pubitemid 30636889)
    • (2000) Journal of Neuroscience , vol.20 , Issue.15 , pp. 5630-5638
    • Paul, S.1    Snyder, G.L.2    Yokakura, H.3    Picciotto, M.R.4    Nairn, A.C.5    Lombroso, P.J.6
  • 45
    • 0034851713 scopus 로고    scopus 로고
    • Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK
    • Du, Q. S., Ren, X. R., Xie, Y., Wang, Q., Mei, L., and Xiong, W. C. (2001) Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK. J. Cell Sci. 114, 2977-2987 (Pubitemid 32821536)
    • (2001) Journal of Cell Science , vol.114 , Issue.16 , pp. 2977-2987
    • Du, Q.-S.1    Ren, X.-R.2    Xie, Y.3    Wang, Q.4    Mei, L.5    Xiong, W.-C.6
  • 46
    • 3042730952 scopus 로고    scopus 로고
    • Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites
    • DOI 10.1242/jcs.01148
    • Haglund, K., Ivankovic-Dikic, I., Shimokawa, N., Kruh, G. D., and Dikic, I. (2004) Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites. J. Cell Sci. 117, 2557-2568 (Pubitemid 38877851)
    • (2004) Journal of Cell Science , vol.117 , Issue.12 , pp. 2557-2568
    • Haglund, K.1    Ivankovic-Dikic, I.2    Shimokawa, N.3    Kruh, G.D.4    Dikic, I.5
  • 47
    • 0035800543 scopus 로고    scopus 로고
    • NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion
    • DOI 10.1016/S0006-8993(01)02619-1, PII S0006899301026191
    • Liu, Y., Zhang, G., Gao, C., and Hou, X. (2001)NMDAreceptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A (NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion. Brain Res. 909, 51-58 (Pubitemid 32710117)
    • (2001) Brain Research , vol.909 , Issue.1-2 , pp. 51-58
    • Liu, Y.1    Zhang, G.2    Gao, C.3    Hou, X.4
  • 48
    • 3242656164 scopus 로고    scopus 로고
    • Lithium suppressed Tyr-402 phosphorylation of proline-rich tyrosine kinase (Pyk2) and interactions of Pyk2 and PSD-95 with NR2A in rat hippocampus following cerebral ischemia
    • DOI 10.1016/j.neures.2004.04.004, PII S0168010204001075
    • Ma, J., Zhang, G. Y., Liu, Y., Yan, J. Z., and Hao, Z. B. (2004) Lithium suppressed Tyr-402 phosphorylation of proline-rich tyrosine kinase (Pyk2) and interactions of Pyk2 and PSD-95 with NR2A in rat hippocampus following cerebral ischemia. Neurosci. Res. 49, 357-362 (Pubitemid 38953852)
    • (2004) Neuroscience Research , vol.49 , Issue.4 , pp. 357-362
    • Ma, J.1    Zhang, G.-Y.2    Liu, Y.3    Yan, J.-Z.4    Hao, Z.-B.5
  • 49
    • 1542287195 scopus 로고    scopus 로고
    • 2+ channel activation mediate proline-rich tyrosine kinase 2 phosphorylation during cerebral ischemia in rats
    • 2+ channel activation mediate proline-rich tyrosine kinase 2 phosphorylation during cerebral ischemia in rats. Neurosci. Lett. 355, 177-180
    • (2004) Neurosci. Lett. , vol.355 , pp. 177-180
    • Guo, J.1    Meng, F.2    Fu, X.3    Song, B.4    Yan, X.5    Zhang, G.6
  • 50
    • 0035827528 scopus 로고    scopus 로고
    • Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade
    • Andreev, J., Galisteo, M. L., Kranenburg, O., Logan, S. K., Chiu, E. S., Okigaki, M., Cary, L. A., Moolenaar, W. H., and Schlessinger, J. (2001) Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade. J. Biol. Chem. 276, 20130-20135
    • (2001) J. Biol. Chem. , vol.276 , pp. 20130-20135
    • Andreev, J.1    Galisteo, M.L.2    Kranenburg, O.3    Logan, S.K.4    Chiu, E.S.5    Okigaki, M.6    Cary, L.A.7    Moolenaar, W.H.8    Schlessinger, J.9
  • 51
    • 77950579398 scopus 로고    scopus 로고
    • The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems
    • Collins, M., Tremblay, M., Chapman, N., Curtiss, M., Rothman, P. B., and Houtman, J. C. (2010) The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems. J. Leukoc. Biol. 87, 691-701
    • (2010) J. Leukoc. Biol. , vol.87 , pp. 691-701
    • Collins, M.1    Tremblay, M.2    Chapman, N.3    Curtiss, M.4    Rothman, P.B.5    Houtman, J.C.6
  • 52
    • 84862289008 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 53
    • 0037561152 scopus 로고    scopus 로고
    • Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102
    • DOI 10.1074/jbc.M212825200
    • Seabold, G. K., Burette, A., Lim, I. A., Weinberg, R. J., and Hell, J. W. (2003) Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102. J. Biol. Chem. 278, 15040-15048 (Pubitemid 36799837)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 15040-15048
    • Seabold, G.K.1    Burette, A.2    Lim, I.A.3    Weinberg, R.J.4    Hell, J.W.5
  • 54
    • 0028857858 scopus 로고
    • Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: A light and electron microscopic study with a complementary DNA-generated polyclonal antibody
    • Oyama, T., Goto, S., Nishi, T., Sato, K., Yamada, K., Yoshikawa, M., and Ushio, Y. (1995) Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: a light and electron microscopic study with a complementary DNA-generated polyclonal antibody. Neuroscience 69, 869-880
    • (1995) Neuroscience , vol.69 , pp. 869-880
    • Oyama, T.1    Goto, S.2    Nishi, T.3    Sato, K.4    Yamada, K.5    Yoshikawa, M.6    Ushio, Y.7
  • 56
    • 33746366493 scopus 로고    scopus 로고
    • Synaptic plasticity: one STEP at a time
    • DOI 10.1016/j.tins.2006.06.007, PII S0166223606001214
    • Braithwaite, S. P., Paul, S., Nairn, A. C., and Lombroso, P. J. (2006) Synaptic plasticity: one STEP at a time. Trends Neurosci. 29, 452-458 (Pubitemid 44118442)
    • (2006) Trends in Neurosciences , vol.29 , Issue.8 , pp. 452-458
    • Braithwaite, S.P.1    Paul, S.2    Nairn, A.C.3    Lombroso, P.J.4
  • 57
  • 58
    • 1642536318 scopus 로고    scopus 로고
    • Dopamine D1-Dependent Trafficking of Striatal N-Methyl-D-aspartate Glutamate Receptors Requires Fyn Protein Tyrosine Kinase but Not DARPP-32
    • DOI 10.1124/mol.65.1.121
    • Dunah, A. W., Sirianni, A. C., Fienberg, A. A., Bastia, E., Schwarzschild, M. A., and Standaert, D. G. (2004) Dopamine D1-dependent trafficking of striatal N-methyl-D-aspartate glutamate receptors requires Fyn protein tyrosine kinase but not DARPP-32. Mol. Pharmacol. 65, 121-129 (Pubitemid 38113892)
    • (2004) Molecular Pharmacology , vol.65 , Issue.1 , pp. 121-129
    • Dunah, A.W.1    Sirianni, A.C.2    Fienberg, A.A.3    Bastia, E.4    Schwarzschild, M.A.5    Standaert, D.G.6
  • 59
    • 33646824867 scopus 로고    scopus 로고
    • 1 activation potentiates striatal NMDA receptors by tyrosine phosphorylation-dependent subunit trafficking
    • DOI 10.1523/JNEUROSCI.0792-06.2006
    • Hallett, P. J., Spoelgen, R., Hyman, B. T., Standaert, D. G., and Dunah, A. W. (2006) Dopamine D1 activation potentiates striatal NMDA receptors by tyrosine phosphorylation-dependent subunit trafficking. J. Neurosci. 26, 4690-4700 (Pubitemid 44315370)
    • (2006) Journal of Neuroscience , vol.26 , Issue.17 , pp. 4690-4700
    • Hallett, P.J.1    Spoelgen, R.2    Hyman, B.T.3    Standaert, D.G.4    Dunah, A.W.5
  • 62
    • 0021162349 scopus 로고
    • DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1
    • Hemmings, H. C., Jr., Greengard, P., Tung, H. Y., and Cohen, P. (1984) DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1. Nature 310, 503-505 (Pubitemid 14052413)
    • (1984) Nature , vol.310 , Issue.5977 , pp. 503-505
    • Hemmings Jr., H.C.1    Greengard, P.2    Lim, T.H.Y.3    Cohen, P.4
  • 63
    • 0033010457 scopus 로고    scopus 로고
    • Role of calcineurin and protein phosphatase-2A in the regulation of DARPP-32 dephosphorylation in neostriatal neurons
    • DOI 10.1046/j.1471-4159.1999.0722015.x
    • Nishi, A., Snyder, G. L., Nairn, A. C., and Greengard, P. (1999) Role of calcineurin and protein phosphatase-2A in the regulation of DARPP-32 dephosphorylation in neostriatal neurons. J. Neurochem. 72, 2015-2021 (Pubitemid 29186005)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.5 , pp. 2015-2021
    • Nishi, A.1    Snyder, G.L.2    Nairn, A.C.3    Greengard, P.4
  • 66
    • 0029112459 scopus 로고
    • Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase
    • Shiozuka, K., Watanabe, Y., Ikeda, T., Hashimoto, S., and Kawashima, H. (1995) Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase. Gene 162, 279-284
    • (1995) Gene , vol.162 , pp. 279-284
    • Shiozuka, K.1    Watanabe, Y.2    Ikeda, T.3    Hashimoto, S.4    Kawashima, H.5
  • 68


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