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Volumn 34, Issue 3, 2007, Pages 355-365

Survival response-linked Pyk2 activation during potassium depletion-induced apoptosis of cerebellar granule neurons

Author keywords

Apoptosis; Calmodulin; Cerebellar granule neurons; Membrane depolarization; Potassium depletion; Pyk2

Indexed keywords

CALCIUM; CALMODULIN; FOCAL ADHESION KINASE 2; POTASSIUM CHLORIDE; TYROSINE;

EID: 33847401361     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2006.11.012     Document Type: Article
Times cited : (6)

References (72)
  • 2
    • 0035910411 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathway in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinases apoptosis
    • Avdi N.J., Nick J.A., Whitlock B.B., Billstrom M.A., Henson P.M., Johnson G.L., and Worthen G.S. Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathway in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinases apoptosis. J. Biol. Chem. 276 (2001) 2189-2199
    • (2001) J. Biol. Chem. , vol.276 , pp. 2189-2199
    • Avdi, N.J.1    Nick, J.A.2    Whitlock, B.B.3    Billstrom, M.A.4    Henson, P.M.5    Johnson, G.L.6    Worthen, G.S.7
  • 5
    • 18144400599 scopus 로고    scopus 로고
    • Implication of phospholipase D2 in oxidant-induced phosphoinositide 3-kinase signaling via Pyk2 activation in PC12 cells
    • Banno Y., Ohguchi K., Matsumoto N., Koda M., Ueda M., Hara A., Dikic I., and Nozawa Y. Implication of phospholipase D2 in oxidant-induced phosphoinositide 3-kinase signaling via Pyk2 activation in PC12 cells. J. Biol. Chem. 280 (2005) 16319-16324
    • (2005) J. Biol. Chem. , vol.280 , pp. 16319-16324
    • Banno, Y.1    Ohguchi, K.2    Matsumoto, N.3    Koda, M.4    Ueda, M.5    Hara, A.6    Dikic, I.7    Nozawa, Y.8
  • 6
    • 0034629082 scopus 로고    scopus 로고
    • Interleukin (IL)-7 induces rapid activation of Pyk2, which is bound to Janus kinase 1 and IL-7Ralpha
    • Benbernou N., Muegge K., and Durum S.K. Interleukin (IL)-7 induces rapid activation of Pyk2, which is bound to Janus kinase 1 and IL-7Ralpha. J. Biol. Chem. 275 (2000) 7060-7065
    • (2000) J. Biol. Chem. , vol.275 , pp. 7060-7065
    • Benbernou, N.1    Muegge, K.2    Durum, S.K.3
  • 7
    • 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., Gronroos E., Dolfi F., Tokiwa G., Vuori K., and Dikic I. Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades. J. Biol. Chem. 274 (1999) 14893-14901
    • (1999) J. Biol. Chem. , vol.274 , pp. 14893-14901
    • Blaukat, A.1    Ivankovic-Dikic, I.2    Gronroos, E.3    Dolfi, F.4    Tokiwa, G.5    Vuori, K.6    Dikic, I.7
  • 8
    • 0033005133 scopus 로고    scopus 로고
    • Depolarization regulates cyclin D1 degradation and neuronal apoptosis: a hypothesis about the role of the ubiquitin/proteasome signalling pathway
    • Boutillier A.L., Kienlen-Campard P., and Loeffler J.P. Depolarization regulates cyclin D1 degradation and neuronal apoptosis: a hypothesis about the role of the ubiquitin/proteasome signalling pathway. Eur. J. Neurosci. 11 (1999) 441-448
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 441-448
    • Boutillier, A.L.1    Kienlen-Campard, P.2    Loeffler, J.P.3
  • 9
    • 0023948929 scopus 로고
    • Dihydropyridine binding sites regulate calcium influx through specific voltage-sensitive calcium channels in cerebellar granule cells
    • Carboni E., and Wojcik W.J. Dihydropyridine binding sites regulate calcium influx through specific voltage-sensitive calcium channels in cerebellar granule cells. J. Neurochem. 50 (1988) 1279-1286
    • (1988) J. Neurochem. , vol.50 , pp. 1279-1286
    • Carboni, E.1    Wojcik, W.J.2
  • 11
    • 12844275929 scopus 로고    scopus 로고
    • Depolarization activates ERK and proline-rich tyrosine kinase 2 (PYK2) independently in different cellular compartments in hippocampal slices
    • Corvol J.C., Valjent E., Toutant M., Enslen H., Irinopoulou T., Lev S., Herve D., and Girault J.A. Depolarization activates ERK and proline-rich tyrosine kinase 2 (PYK2) independently in different cellular compartments in hippocampal slices. J. Biol. Chem. 280 (2005) 660-668
    • (2005) J. Biol. Chem. , vol.280 , 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
  • 12
    • 0025580921 scopus 로고
    • The interactions between plasma membrane depolarization and glutamate receptor activation in the regulation of cytoplasmic free calcium in cultured cerebellar granule cells
    • Courtney M.J., Lambert J.J., and Nicholls D.G. The interactions between plasma membrane depolarization and glutamate receptor activation in the regulation of cytoplasmic free calcium in cultured cerebellar granule cells. J. Neurosci. 10 (1990) 3873-3879
    • (1990) J. Neurosci. , vol.10 , pp. 3873-3879
    • Courtney, M.J.1    Lambert, J.J.2    Nicholls, D.G.3
  • 13
    • 0030872062 scopus 로고    scopus 로고
    • Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors. Convergence of Gi- and Gq-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase
    • Della Rocca G.J., van Biesen T., Daaka Y., Luttrell D.K., Luttrell L.M., and Lefkowitz R.J. Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors. Convergence of Gi- and Gq-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase. J. Biol. Chem. 272 (1997) 19125-19132
    • (1997) J. Biol. Chem. , vol.272 , pp. 19125-19132
    • Della Rocca, G.J.1    van Biesen, T.2    Daaka, Y.3    Luttrell, D.K.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 15
    • 0031814171 scopus 로고    scopus 로고
    • Differential regulation of FAK+ and PYK2/Cakbeta, two related tyrosine kinases, in rat hippocampal slices: effects of LPA, carbachol, depolarization and hyperosmolarity
    • Derkinderen P., Siciliano J., Toutant M., and Girault J.A. Differential regulation of FAK+ and PYK2/Cakbeta, two related tyrosine kinases, in rat hippocampal slices: effects of LPA, carbachol, depolarization and hyperosmolarity. Eur. J. Neurosci. 10 (1998) 1667-1675
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1667-1675
    • Derkinderen, P.1    Siciliano, J.2    Toutant, M.3    Girault, J.A.4
  • 16
    • 14044270949 scopus 로고    scopus 로고
    • Genes regulated in neurons undergoing transcription-dependent apoptosis belong to signaling pathways rather than the apoptotic machinery
    • Desagher S., Severac D., Lipkin A., Bernis C., Ritchie W., Le Digarcher A., and Journot L. Genes regulated in neurons undergoing transcription-dependent apoptosis belong to signaling pathways rather than the apoptotic machinery. J. Biol. Chem. 280 (2005) 5693-5702
    • (2005) J. Biol. Chem. , vol.280 , pp. 5693-5702
    • Desagher, S.1    Severac, D.2    Lipkin, A.3    Bernis, C.4    Ritchie, W.5    Le Digarcher, A.6    Journot, L.7
  • 17
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic I., Tokiwa G., Lev S., Courtneidge S.A., and Schlessinger J. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383 (1996) 547-550
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 18
    • 0027483920 scopus 로고
    • Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP
    • D'Mello S.R., Galli C., Ciotti T., and Calissano P. Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 10989-10993
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 10989-10993
    • D'Mello, S.R.1    Galli, C.2    Ciotti, T.3    Calissano, P.4
  • 19
    • 0024205540 scopus 로고
    • Modulation of calcium current by calmodulin antagonists
    • Doroshenko P.A., Kostyuk P.G., and Luk'yanetz E.A. Modulation of calcium current by calmodulin antagonists. Neuroscience 27 (1988) 1073-1080
    • (1988) Neuroscience , vol.27 , pp. 1073-1080
    • Doroshenko, P.A.1    Kostyuk, P.G.2    Luk'yanetz, E.A.3
  • 20
    • 3042818863 scopus 로고    scopus 로고
    • Mitochondrial signals initiate the activation of c-Jun N-terminal kinase (JNK) by hypoxia-reoxygenation
    • Dougherty C.J., Kubasiak L.A., Frazier D.P., Li H., Xiong W.C., Bishopric N.H., and Webster K.A. Mitochondrial signals initiate the activation of c-Jun N-terminal kinase (JNK) by hypoxia-reoxygenation. FASEB J. 18 (2004) 1060-1070
    • (2004) FASEB J. , vol.18 , pp. 1060-1070
    • Dougherty, C.J.1    Kubasiak, L.A.2    Frazier, D.P.3    Li, H.4    Xiong, W.C.5    Bishopric, N.H.6    Webster, K.A.7
  • 22
    • 0026482631 scopus 로고
    • Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium
    • Franklin J.L., and Johnson Jr. E.M. Suppression of programmed neuronal death by sustained elevation of cytoplasmic calcium. Trends Neurosci. 15 (1992) 501-508
    • (1992) Trends Neurosci. , vol.15 , pp. 501-508
    • Franklin, J.L.1    Johnson Jr., E.M.2
  • 23
    • 0028831283 scopus 로고
    • Chronic depolarization prevents programmed death of sympathetic neurons in vitro but does not support growth: requirement for Ca2+ influx but not Trk activation
    • Franklin J.L., Sanz-Rodriguez C., Juhasz A., Deckwerth T.L., and Johnson Jr. E.M. Chronic depolarization prevents programmed death of sympathetic neurons in vitro but does not support growth: requirement for Ca2+ influx but not Trk activation. J. Neurosci. 15 (1995) 643-664
    • (1995) J. Neurosci. , vol.15 , pp. 643-664
    • Franklin, J.L.1    Sanz-Rodriguez, C.2    Juhasz, A.3    Deckwerth, T.L.4    Johnson Jr., E.M.5
  • 24
    • 0023244774 scopus 로고
    • The role of depolarization in the survival and differentiation of cerebellar granule cells in culture
    • Gallo V., Kingsbury A., Balazs R., and Jorgensen O.S. The role of depolarization in the survival and differentiation of cerebellar granule cells in culture. J. Neurosci. 7 (1987) 2203-2213
    • (1987) J. Neurosci. , vol.7 , pp. 2203-2213
    • Gallo, V.1    Kingsbury, A.2    Balazs, R.3    Jorgensen, O.S.4
  • 25
    • 0036080595 scopus 로고    scopus 로고
    • CaM kinase II-dependent activation of tyrosine kinases and ERK1/2 in vascular smooth muscle
    • Ginnan R., and Singer H.A. CaM kinase II-dependent activation of tyrosine kinases and ERK1/2 in vascular smooth muscle. Am. J. Physiol.: Cell Physiol. 282 (2002) C754-C761
    • (2002) Am. J. Physiol.: Cell Physiol. , vol.282
    • Ginnan, R.1    Singer, H.A.2
  • 26
    • 0032586727 scopus 로고    scopus 로고
    • FAK and PYK2/CAKbeta in the nervous system: a link between neuronal activity, plasticity and survival?
    • Girault J.A., Costa A., Derkinderen P., Studler J.M., and Toutant M. FAK and PYK2/CAKbeta in the nervous system: a link between neuronal activity, plasticity and survival?. Trends Neurosci. 22 (1999) 257-263
    • (1999) Trends Neurosci. , vol.22 , pp. 257-263
    • Girault, J.A.1    Costa, A.2    Derkinderen, P.3    Studler, J.M.4    Toutant, M.5
  • 27
    • 0023135942 scopus 로고
    • Interaction of calmodulin inhibitors and protein kinase C inhibitors with voltage-dependent calcium channels
    • Greenberg D.A., Carpenter C.L., and Messing R.O. Interaction of calmodulin inhibitors and protein kinase C inhibitors with voltage-dependent calcium channels. Brain Res. 404 (1987) 401-404
    • (1987) Brain Res. , vol.404 , pp. 401-404
    • Greenberg, D.A.1    Carpenter, C.L.2    Messing, R.O.3
  • 28
    • 1542287195 scopus 로고    scopus 로고
    • N-methyl-d-aspartate receptor and L-type voltage-gated Ca2+ channel activation mediate proline-rich tyrosine kinase 2 phosphorylation during cerebral ischemia in rats
    • Guo J., Meng F., Fu X., Song B., Yan X., and Zhang G. N-methyl-d-aspartate receptor and L-type voltage-gated Ca2+ channel activation mediate proline-rich tyrosine kinase 2 phosphorylation during cerebral ischemia in rats. Neurosci. Lett. 355 (2004) 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
  • 29
    • 0027504455 scopus 로고
    • Promotion of granule cell survival by high K+ or excitatory amino acid treatment and Ca2+/calmodulin-dependent protein kinase activity
    • Hack N., Hidaka H., Wakefield M.J., and Balazs R. Promotion of granule cell survival by high K+ or excitatory amino acid treatment and Ca2+/calmodulin-dependent protein kinase activity. Neuroscience 57 (1993) 9-20
    • (1993) Neuroscience , vol.57 , pp. 9-20
    • Hack, N.1    Hidaka, H.2    Wakefield, M.J.3    Balazs, R.4
  • 30
    • 0036662898 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: mediation through the Pyk2/Src-family kinase pathway in cortical neurons
    • Heidinger V., Manzerra P., Wang X.Q., Strasser U., Yu S.P., Choi D.W., and Behrens M.M. Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: mediation through the Pyk2/Src-family kinase pathway in cortical neurons. J. Neurosci. 22 (2002) 5452-5461
    • (2002) J. Neurosci. , vol.22 , pp. 5452-5461
    • Heidinger, V.1    Manzerra, P.2    Wang, X.Q.3    Strasser, U.4    Yu, S.P.5    Choi, D.W.6    Behrens, M.M.7
  • 31
    • 0029978069 scopus 로고    scopus 로고
    • Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization
    • Herzog H., Nicholl J., Hort Y.J., Sutherland G.R., and Shine J. Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization. Genomics 32 (1996) 484-486
    • (1996) Genomics , vol.32 , pp. 484-486
    • Herzog, H.1    Nicholl, J.2    Hort, Y.J.3    Sutherland, G.R.4    Shine, J.5
  • 32
    • 0020643734 scopus 로고
    • Naphthalenesulfonamides as calmodulin antagonists
    • Hidaka H., and Tanaka T. Naphthalenesulfonamides as calmodulin antagonists. Methods Enzymol. 102 (1983) 185-194
    • (1983) Methods Enzymol. , vol.102 , pp. 185-194
    • Hidaka, H.1    Tanaka, T.2
  • 34
  • 35
    • 0024711746 scopus 로고
    • Role of Ca2+ channels in the ability of membrane depolarization to prevent neuronal death induced by trophic-factor deprivation: evidence that levels of internal Ca2+ determine nerve growth factor dependence of sympathetic ganglion cells
    • Koike T., Martin D.P., and Johnson Jr. E.M. Role of Ca2+ channels in the ability of membrane depolarization to prevent neuronal death induced by trophic-factor deprivation: evidence that levels of internal Ca2+ determine nerve growth factor dependence of sympathetic ganglion cells. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 6421-6425
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6421-6425
    • Koike, T.1    Martin, D.P.2    Johnson Jr., E.M.3
  • 36
    • 0034934786 scopus 로고    scopus 로고
    • RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase
    • Koziak K., Kaczmarek E., Park S.Y., Fu Y., Avraham S., and Avraham H. RAFTK/Pyk2 involvement in platelet activation is mediated by phosphoinositide 3-kinase. Br. J. Haematol. 114 (2001) 134-140
    • (2001) Br. J. Haematol. , vol.114 , pp. 134-140
    • Koziak, K.1    Kaczmarek, E.2    Park, S.Y.3    Fu, Y.4    Avraham, S.5    Avraham, H.6
  • 37
    • 0036460434 scopus 로고    scopus 로고
    • Akt mediates the anti-apoptotic effect of NMDA but not that induced by potassium depolarization in cultured cerebellar granule cells
    • Lafon-Cazal M., Perez V., Bockaert J., and Marin P. Akt mediates the anti-apoptotic effect of NMDA but not that induced by potassium depolarization in cultured cerebellar granule cells. Eur. J. Neurosci. 16 (2002) 575-583
    • (2002) Eur. J. Neurosci. , vol.16 , pp. 575-583
    • Lafon-Cazal, M.1    Perez, V.2    Bockaert, J.3    Marin, P.4
  • 39
    • 0033605594 scopus 로고    scopus 로고
    • Interactions between two cytoskeleton-associated tyrosine kinases: calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase
    • Li X., Dy R.C., Cance W.G., Graves L.M., and Earp H.S. Interactions between two cytoskeleton-associated tyrosine kinases: calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase. J. Biol. Chem. 274 (1999) 8917-8924
    • (1999) J. Biol. Chem. , vol.274 , pp. 8917-8924
    • Li, X.1    Dy, R.C.2    Cance, W.G.3    Graves, L.M.4    Earp, H.S.5
  • 40
    • 11144234830 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin
    • Melendez J., Turner C., Avraham H., Steinberg S.F., Schaefer E., and Sussman M.A. Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin. J. Biol. Chem. 279 (2004) 53516-53523
    • (2004) J. Biol. Chem. , vol.279 , pp. 53516-53523
    • Melendez, J.1    Turner, C.2    Avraham, H.3    Steinberg, S.F.4    Schaefer, E.5    Sussman, M.A.6
  • 41
    • 3142615409 scopus 로고    scopus 로고
    • The cytoplasmic tyrosine kinase Pyk2 as a novel effector of fibroblast growth factor receptor 3 activation
    • Meyer A.N., Gastwirt R.F., Schlaepfer D.D., and Donoghue D.J. The cytoplasmic tyrosine kinase Pyk2 as a novel effector of fibroblast growth factor receptor 3 activation. J. Biol. Chem. 279 (2004) 28450-28457
    • (2004) J. Biol. Chem. , vol.279 , pp. 28450-28457
    • Meyer, A.N.1    Gastwirt, R.F.2    Schlaepfer, D.D.3    Donoghue, D.J.4
  • 42
    • 0029909560 scopus 로고    scopus 로고
    • Metabolic and genetic analyses of apoptosis in potassium/serum-deprived rat cerebellar granule cells
    • Miller T.M., and Johnson Jr. E.M. Metabolic and genetic analyses of apoptosis in potassium/serum-deprived rat cerebellar granule cells. J. Neurosci. 16 (1996) 7487-7495
    • (1996) J. Neurosci. , vol.16 , pp. 7487-7495
    • Miller, T.M.1    Johnson Jr., E.M.2
  • 43
    • 0030938816 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase activity blocks depolarization- and insulin-like growth factor I-mediated survival of cerebellar granule cells
    • Miller T.M., Tansey M.G., Johnson Jr. E.M., and Creedon D.J. Inhibition of phosphatidylinositol 3-kinase activity blocks depolarization- and insulin-like growth factor I-mediated survival of cerebellar granule cells. J. Biol. Chem. 272 (1997) 9847-9853
    • (1997) J. Biol. Chem. , vol.272 , pp. 9847-9853
    • Miller, T.M.1    Tansey, M.G.2    Johnson Jr., E.M.3    Creedon, D.J.4
  • 44
    • 0033043513 scopus 로고    scopus 로고
    • Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein
    • Missotten M., Nichols A., Rieger K., and Sadoul R. Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ. 6 (1999) 124-129
    • (1999) Cell Death Differ. , vol.6 , pp. 124-129
    • Missotten, M.1    Nichols, A.2    Rieger, K.3    Sadoul, R.4
  • 45
    • 0035800625 scopus 로고    scopus 로고
    • Discovery of a novel compound: insight into mechanisms for acrylamide-induced axonopathy and colchicine-induced apoptotic neuronal cell death
    • Nakagawa-Yagi Y., Choi D.K., Ogane N., Shimada S., Seya M., Momoi T., Ito T., and Sakaki Y. Discovery of a novel compound: insight into mechanisms for acrylamide-induced axonopathy and colchicine-induced apoptotic neuronal cell death. Brain Res. 909 (2001) 8-19
    • (2001) Brain Res. , vol.909 , pp. 8-19
    • Nakagawa-Yagi, Y.1    Choi, D.K.2    Ogane, N.3    Shimada, S.4    Seya, M.5    Momoi, T.6    Ito, T.7    Sakaki, Y.8
  • 48
    • 0033605421 scopus 로고    scopus 로고
    • Bcl-xL blocks activation of related adhesion focal tyrosine kinase/proline-rich tyrosine kinase 2 and stress-activated protein kinase/c-Jun N-terminal protein kinase in the cellular response to methylmethane sulfonate
    • Pandey P., Avraham S., Place A., Kumar V., Majumder P.K., Cheng K., Nakazawa A., Saxena S., and Kharbanda S. Bcl-xL blocks activation of related adhesion focal tyrosine kinase/proline-rich tyrosine kinase 2 and stress-activated protein kinase/c-Jun N-terminal protein kinase in the cellular response to methylmethane sulfonate. J. Biol. Chem. 274 (1999) 8618-8623
    • (1999) J. Biol. Chem. , vol.274 , pp. 8618-8623
    • Pandey, P.1    Avraham, S.2    Place, A.3    Kumar, V.4    Majumder, P.K.5    Cheng, K.6    Nakazawa, A.7    Saxena, S.8    Kharbanda, S.9
  • 49
    • 0034683229 scopus 로고    scopus 로고
    • Protein kinase A activity is required for depolarization-induced proline-rich tyrosine kinase 2 and mitogen-activated protein kinase activation in PC12 cells
    • Park J.H., Park J.K., Bae K.W., and Park H.T. Protein kinase A activity is required for depolarization-induced proline-rich tyrosine kinase 2 and mitogen-activated protein kinase activation in PC12 cells. Neurosci. Lett. 290 (2000) 25-28
    • (2000) Neurosci. Lett. , vol.290 , pp. 25-28
    • Park, J.H.1    Park, J.K.2    Bae, K.W.3    Park, H.T.4
  • 50
    • 0034733540 scopus 로고    scopus 로고
    • Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation
    • Park S.Y., Avraham H., and Avraham S. Characterization of the tyrosine kinases RAFTK/Pyk2 and FAK in nerve growth factor-induced neuronal differentiation. J. Biol. Chem. 275 (2000) 19768-19777
    • (2000) J. Biol. Chem. , vol.275 , pp. 19768-19777
    • Park, S.Y.1    Avraham, H.2    Avraham, S.3
  • 51
    • 4043054389 scopus 로고    scopus 로고
    • RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner
    • Park S.Y., Avraham H.K., and Avraham S. RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner. J. Biol. Chem. 279 (2004) 33315-33322
    • (2004) J. Biol. Chem. , vol.279 , pp. 33315-33322
    • Park, S.Y.1    Avraham, H.K.2    Avraham, S.3
  • 53
    • 0035413357 scopus 로고    scopus 로고
    • MIP-1alpha induces activation of phosphatidylinositol-3 kinase that associates with Pyk-2 and is necessary for B-cell migration
    • Rumsey L.M., Teague R.M., Benedict S.H., and Chan M.A. MIP-1alpha induces activation of phosphatidylinositol-3 kinase that associates with Pyk-2 and is necessary for B-cell migration. Exp. Cell Res. 268 (2001) 77-83
    • (2001) Exp. Cell Res. , vol.268 , pp. 77-83
    • Rumsey, L.M.1    Teague, R.M.2    Benedict, S.H.3    Chan, M.A.4
  • 54
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., and Sasaki T. Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J. Biol. Chem. 270 (1995) 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
  • 55
    • 0034058884 scopus 로고    scopus 로고
    • Thrombin-stimulated phosphatidylinositol 3-kinase activity in platelets is associated with activation of PYK2 tyrosine kinase: activation of both enzymes is aggregation independent
    • Sayed M.R., Sheid M.P., Stevens C.M., and Duronio V. Thrombin-stimulated phosphatidylinositol 3-kinase activity in platelets is associated with activation of PYK2 tyrosine kinase: activation of both enzymes is aggregation independent. J. Cell. Physiol. 183 (2000) 314-320
    • (2000) J. Cell. Physiol. , vol.183 , pp. 314-320
    • Sayed, M.R.1    Sheid, M.P.2    Stevens, C.M.3    Duronio, V.4
  • 56
    • 13544271663 scopus 로고    scopus 로고
    • Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities
    • Schmidt M.H., Dikic I., and Bogler O. Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities. J. Biol. Chem. 280 (2005) 3414-3425
    • (2005) J. Biol. Chem. , vol.280 , pp. 3414-3425
    • Schmidt, M.H.1    Dikic, I.2    Bogler, O.3
  • 57
    • 0035175495 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons
    • See V., Boutillier A.L., Bito H., and Loeffler J.P. Calcium/calmodulin-dependent protein kinase type IV (CaMKIV) inhibits apoptosis induced by potassium deprivation in cerebellar granule neurons. FASEB J. 15 (2001) 134-144
    • (2001) FASEB J. , vol.15 , pp. 134-144
    • See, V.1    Boutillier, A.L.2    Bito, H.3    Loeffler, J.P.4
  • 58
    • 0035943649 scopus 로고    scopus 로고
    • PYK2 links G(q)alpha and G(13)alpha signaling to NF-kappa B activation
    • Shi C.S., and Kehrl J.H. PYK2 links G(q)alpha and G(13)alpha signaling to NF-kappa B activation. J. Biol. Chem. 276 (2001) 31845-31850
    • (2001) J. Biol. Chem. , vol.276 , pp. 31845-31850
    • Shi, C.S.1    Kehrl, J.H.2
  • 59
    • 0033524740 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase activity elevates c-Jun N-terminal kinase activity in apoptosis of cultured cerebellar granule neurons
    • Shimoke K., Yamagishi S., Yamada M., Ikeuchi T., and Hatanaka H. Inhibition of phosphatidylinositol 3-kinase activity elevates c-Jun N-terminal kinase activity in apoptosis of cultured cerebellar granule neurons. Brain Res. Dev. Brain Res. 112 (1999) 245-253
    • (1999) Brain Res. Dev. Brain Res. , vol.112 , pp. 245-253
    • Shimoke, K.1    Yamagishi, S.2    Yamada, M.3    Ikeuchi, T.4    Hatanaka, H.5
  • 60
    • 0029840588 scopus 로고    scopus 로고
    • Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125(FAK) by glutamate and depolarization in rat hippocampus
    • Siciliano J.C., Toutant M., Derkinderen P., Sasaki T., and Girault J.A. Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125(FAK) by glutamate and depolarization in rat hippocampus. J. Biol. Chem. 271 (1996) 28942-28946
    • (1996) J. Biol. Chem. , vol.271 , pp. 28942-28946
    • Siciliano, J.C.1    Toutant, M.2    Derkinderen, P.3    Sasaki, T.4    Girault, J.A.5
  • 61
    • 0032519650 scopus 로고    scopus 로고
    • Calmodulin is involved in membrane depolarization-mediated survival of motoneurons by phosphatidylinositol-3 kinase- and MAPK-independent pathways
    • Soler R.M., Egea J., Mintenig G.M., Sanz-Rodriguez C., Iglesias M., and Comella J.X. Calmodulin is involved in membrane depolarization-mediated survival of motoneurons by phosphatidylinositol-3 kinase- and MAPK-independent pathways. J. Neurosci. 18 (1998) 1230-1239
    • (1998) J. Neurosci. , vol.18 , pp. 1230-1239
    • Soler, R.M.1    Egea, J.2    Mintenig, G.M.3    Sanz-Rodriguez, C.4    Iglesias, M.5    Comella, J.X.6
  • 63
    • 0034281374 scopus 로고    scopus 로고
    • Cerebral ischemia and seizures induce tyrosine phosphorylation of PYK2 in neurons and microglial cells
    • Tian D., Litvak V., and Lev S. Cerebral ischemia and seizures induce tyrosine phosphorylation of PYK2 in neurons and microglial cells. J. Neurosci. 20 (2000) 6478-6487
    • (2000) J. Neurosci. , vol.20 , pp. 6478-6487
    • Tian, D.1    Litvak, V.2    Lev, S.3
  • 64
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G., Dikic I., Lev S., and Schlessinger J. Activation of Pyk2 by stress signals and coupling with JNK signaling pathway. Science 273 (1996) 792-794
    • (1996) Science , vol.273 , pp. 792-794
    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
  • 66
    • 0034678330 scopus 로고    scopus 로고
    • Suppression of Pyk2 kinase and cellular activities by FIP200
    • Ueda H., Abbi S., Zheng C., and Guan J.L. Suppression of Pyk2 kinase and cellular activities by FIP200. J. Cell Biol. 149 (2000) 423-430
    • (2000) J. Cell Biol. , vol.149 , pp. 423-430
    • Ueda, H.1    Abbi, S.2    Zheng, C.3    Guan, J.L.4
  • 67
    • 0033556043 scopus 로고    scopus 로고
    • Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction
    • Vito P., Pellegrini L., Guiet C., and D'Adamio L. Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction. J. Biol. Chem. 274 (1999) 1533-1540
    • (1999) J. Biol. Chem. , vol.274 , pp. 1533-1540
    • Vito, P.1    Pellegrini, L.2    Guiet, C.3    D'Adamio, L.4
  • 68
    • 10944223361 scopus 로고    scopus 로고
    • Altered regulation of Src upon cell detachment protects human lung adenocarcinoma cells from anoikis
    • Wei L., Yang Y., Zhang X., and Yu Q. Altered regulation of Src upon cell detachment protects human lung adenocarcinoma cells from anoikis. Oncogene 23 (2004) 9052-9061
    • (2004) Oncogene , vol.23 , pp. 9052-9061
    • Wei, L.1    Yang, Y.2    Zhang, X.3    Yu, Q.4
  • 69
    • 1542674329 scopus 로고    scopus 로고
    • Roles of FAK family kinases in nervous system
    • Xiong W.C., and Mei L. Roles of FAK family kinases in nervous system. Front. Biosci. 8 (2003) s676-s682
    • (2003) Front. Biosci. , vol.8
    • Xiong, W.C.1    Mei, L.2
  • 70
    • 0030777767 scopus 로고    scopus 로고
    • Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase
    • Xiong W., and Parsons J.T. Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase. J. Cell Biol. 139 (1997) 529-539
    • (1997) J. Cell Biol. , vol.139 , pp. 529-539
    • Xiong, W.1    Parsons, J.T.2
  • 71
    • 0010233279 scopus 로고    scopus 로고
    • Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation
    • Yu H., Li X., Marchetto G.S., Dy R., Hunter D., Calvo B., Dawson T.L., Wilm M., Anderegg R.J., Graves L.M., and Earp H.S. Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation. J. Biol. Chem. 271 (1996) 29993-29998
    • (1996) J. Biol. Chem. , vol.271 , pp. 29993-29998
    • Yu, H.1    Li, X.2    Marchetto, G.S.3    Dy, R.4    Hunter, D.5    Calvo, B.6    Dawson, T.L.7    Wilm, M.8    Anderegg, R.J.9    Graves, L.M.10    Earp, H.S.11
  • 72
    • 0033597859 scopus 로고    scopus 로고
    • Distinct calcium-dependent pathways of epidermal growth factor receptor transactivation and PYK2 tyrosine phosphorylation in PC12 cells
    • Zwick E., Wallasch C., Daub H., and Ullrich A. Distinct calcium-dependent pathways of epidermal growth factor receptor transactivation and PYK2 tyrosine phosphorylation in PC12 cells. J. Biol. Chem. 274 (1999) 20989-20996
    • (1999) J. Biol. Chem. , vol.274 , pp. 20989-20996
    • Zwick, E.1    Wallasch, C.2    Daub, H.3    Ullrich, A.4


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