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Volumn 7, Issue 3, 1997, Pages 419-429

Ca2+-dependent regulation in neuronal gene expression

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; TRANSCRIPTION FACTOR; CALCIUM;

EID: 0030611787     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(97)80072-4     Document Type: Article
Times cited : (254)

References (139)
  • 1
    • 0028902884 scopus 로고
    • Retrograde amnesia and memory consolidation: A neurobiological perspective
    • Squire LR, Alvarez P. Retrograde amnesia and memory consolidation: a neurobiological perspective. Curr Opin Neurobiol. 5:1995;169-177.
    • (1995) Curr Opin Neurobiol , vol.5 , pp. 169-177
    • Squire, L.R.1    Alvarez, P.2
  • 2
    • 0030068504 scopus 로고    scopus 로고
    • Emergence of order in visual system development
    • Shatz CJ. Emergence of order in visual system development. Proc Natl Acad Sci USA. 93:1996;602-608.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 602-608
    • Shatz, C.J.1
  • 3
    • 0030450763 scopus 로고    scopus 로고
    • Toward a molecular definition of long-term memory storage
    • Bailey CH, Bartsch D, Kandel ER. Toward a molecular definition of long-term memory storage. Proc Natl Acad Sci USA. 93:1996;13445-13452.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13445-13452
    • Bailey, C.H.1    Bartsch, D.2    Kandel, E.R.3
  • 4
    • 0028860249 scopus 로고
    • Fos: An immediate-early transcription factor in neurons
    • Curran T, Morgan JI. Fos: an immediate-early transcription factor in neurons. J Neurobiol. 26:1995;403-412.
    • (1995) J Neurobiol , vol.26 , pp. 403-412
    • Curran, T.1    Morgan, J.I.2
  • 5
    • 0027443739 scopus 로고
    • Thresholds for synaptic activation of transcription factors in hippocampus: Correlation with long-term enhancement
    • Worley PF, Bhat RV, Baraban JM, Erickson CA, McNaughton BL, Barnes CA. Thresholds for synaptic activation of transcription factors in hippocampus: correlation with long-term enhancement. J Neurosci. 13:1993;4776-4786.
    • (1993) J Neurosci , vol.13 , pp. 4776-4786
    • Worley, P.F.1    Bhat, R.V.2    Baraban, J.M.3    Erickson, C.A.4    McNaughton, B.L.5    Barnes, C.A.6
  • 6
    • 0028914467 scopus 로고
    • Molecular mechanisms of drug reinforcement and addiction
    • Self DW, Nestler EJ. Molecular mechanisms of drug reinforcement and addiction. Annu Rev Neurosci. 18:1995;463-495.
    • (1995) Annu Rev Neurosci , vol.18 , pp. 463-495
    • Self, D.W.1    Nestler, E.J.2
  • 7
    • 0028579556 scopus 로고
    • Proto-oncogenes: Basic concepts and stimulation induced changes in the spinal cord
    • Munglani R, Hunt SP. Proto-oncogenes: basic concepts and stimulation induced changes in the spinal cord. Prog Brain Res. 104:1995;283-298.
    • (1995) Prog Brain Res , vol.104 , pp. 283-298
    • Munglani, R.1    Hunt, S.P.2
  • 8
    • 0030055163 scopus 로고    scopus 로고
    • A role for immediate-early transcription factors in learning and memory
    • Dragunow M. A role for immediate-early transcription factors in learning and memory. Behav Genet. 26:1996;293-299.
    • (1996) Behav Genet , vol.26 , pp. 293-299
    • Dragunow, M.1
  • 9
    • 0345018279 scopus 로고    scopus 로고
    • Voltage-gated calcium channels
    • E. Carafoli, Klee C.B. New York: Oxford University Press. in press
    • Tsien RW, Wheeler DB. Voltage-gated calcium channels. Carafoli E, Klee CB. Intracellular Calcium. 1997;Oxford University Press, New York. in press.
    • (1997) Intracellular Calcium
    • Tsien, R.W.1    Wheeler, D.B.2
  • 10
    • 0024403534 scopus 로고
    • Rapid increase of an immediate early gene messenger RNA in hippocampal neurons by synaptic NMDA receptor activation
    • Cole AJ, Saffen DW, Baraban JM, Worley PF. Rapid increase of an immediate early gene messenger RNA in hippocampal neurons by synaptic NMDA receptor activation. Nature. 340:1989;474-476.
    • (1989) Nature , vol.340 , pp. 474-476
    • Cole, A.J.1    Saffen, D.W.2    Baraban, J.M.3    Worley, P.F.4
  • 12
    • 0028033340 scopus 로고
    • Spatial and temporal changes in signal transduction pathways during LTP
    • Thomas KL, Laroche S, Errington ML, Bliss TVP, Hunt SP. Spatial and temporal changes in signal transduction pathways during LTP. Neuron. 13:1994;737-745.
    • (1994) Neuron , vol.13 , pp. 737-745
    • Thomas, K.L.1    Laroche, S.2    Errington, M.L.3    Bliss, T.V.P.4    Hunt, S.P.5
  • 13
    • 0027971439 scopus 로고
    • Immediate early gene expression associated with the persistence of heterosynaptic long-term depression in the hippocampus
    • Abraham WC, Christie BR, Logan B, Lawlor P, Dragunow M. Immediate early gene expression associated with the persistence of heterosynaptic long-term depression in the hippocampus. Proc Natl Acad Sci USA. 91:1994;10049-10053.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10049-10053
    • Abraham, W.C.1    Christie, B.R.2    Logan, B.3    Lawlor, P.4    Dragunow, M.5
  • 14
    • 0029898252 scopus 로고    scopus 로고
    • Induction of CRE-mediated gene expression by stimuli that generate long-lasting LTP in area CA1 of the hippocampus
    • 2+ channel blockers were both sufficient to block L-LTP-induced downstream gene expression. of outstanding interest
    • 2+ channel blockers were both sufficient to block L-LTP-induced downstream gene expression. of outstanding interest.
    • (1996) Neuron , vol.16 , pp. 973-982
    • Impey, S.1    Mark, M.2    Villacres, E.C.3    Poser, S.4    Chavkin, C.5    Storm, D.R.6
  • 15
    • 0030059338 scopus 로고    scopus 로고
    • Signaling from synapse to nucleus: Postsynaptic CREB phosphorylation during multiple forms of hippocampal synaptic plasticity
    • 2+ effector that was BAPTA-sensitive but EGTA-insensitive. of outstanding interest
    • 2+ effector that was BAPTA-sensitive but EGTA-insensitive. of outstanding interest.
    • (1996) Neuron , vol.16 , pp. 89-101
    • Deisseroth, K.1    Bito, H.2    Tsien, R.W.3
  • 16
    • 0028972042 scopus 로고
    • 2+-dependent inactivation of calcineurin in brain
    • See annotation [17]. of outstanding interest of special interest
    • 2+-dependent inactivation of calcineurin in brain. FEBS Lett. 374:1995;237-240 See annotation [17]. of outstanding interest of special interest.
    • (1995) FEBS Lett , vol.374 , pp. 237-240
    • Stemmer, P.M.1    Wang, X.2    Krinks, M.H.3    Klee, C.B.4
  • 17
    • 0029759409 scopus 로고    scopus 로고
    • Superoxide dismutase protects calcineurin from inactivation
    • 2+/CaM. In this paper [17], they show that this process is prevented by combining superoxide dismutase (SOD) with calcineurin. Genetic disruption of SOD in yeast is associated with a significant loss of calcineurin activity. The phenotype of the SOD-deficient yeast was similar to that seen in calcineurin mutants. of special interest of outstanding interest
    • 2+/CaM. In this paper [17], they show that this process is prevented by combining superoxide dismutase (SOD) with calcineurin. Genetic disruption of SOD in yeast is associated with a significant loss of calcineurin activity. The phenotype of the SOD-deficient yeast was similar to that seen in calcineurin mutants. of special interest of outstanding interest.
    • (1996) Nature , vol.383 , pp. 434-437
    • Wang, X.1    Culotta, V.C.2    Klee, C.B.3
  • 19
    • 0031024891 scopus 로고    scopus 로고
    • Synaptic tagging and long-term potentiation
    • A reversible post-translational synaptic modification (tagging) confers synaptic specificity for L-LTP by recruiting a protein-synthesis-dependent factor induced during L-LTP. of outstanding interest
    • Frey U, Morris RGM. Synaptic tagging and long-term potentiation. Nature. 385:1997;533-536 A reversible post-translational synaptic modification (tagging) confers synaptic specificity for L-LTP by recruiting a protein-synthesis-dependent factor induced during L-LTP. of outstanding interest.
    • (1997) Nature , vol.385 , pp. 533-536
    • Frey, U.1    Morris, R.G.M.2
  • 20
    • 0025807509 scopus 로고
    • 2+-regulated transcription factor phosphorylated by calmodulin-dependent kinases
    • 2+-regulated transcription factor phosphorylated by calmodulin-dependent kinases. Science. 252:1991;1427-1430.
    • (1991) Science , vol.252 , pp. 1427-1430
    • Sheng, M.1    Thompson, M.A.2    Greenberg, M.E.3
  • 22
    • 0027968663 scopus 로고
    • Roles of calmodulin-dependent protein kinases and phosphatase in calcium-dependent transcription of immediate early genes
    • Enslen H, Soderling TR. Roles of calmodulin-dependent protein kinases and phosphatase in calcium-dependent transcription of immediate early genes. J Biol Chem. 269:1994;20872-20877.
    • (1994) J Biol Chem , vol.269 , pp. 20872-20877
    • Enslen, H.1    Soderling, T.R.2
  • 23
    • 0028787753 scopus 로고
    • Multiple protein kinase A-regulated events are required for transcriptional induction by cAMP
    • Brindle P, Nakajima T, Montminy M. Multiple protein kinase A-regulated events are required for transcriptional induction by cAMP. Proc Natl Acad Sci USA. 92:1995;10521-10525.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10521-10525
    • Brindle, P.1    Nakajima, T.2    Montminy, M.3
  • 25
    • 0029855061 scopus 로고    scopus 로고
    • Stimulus-transcription coupling in pheochromocytoma cells. Promoter region-specific activation of chromogranin A biosynthesis
    • Tang K, Wu H, Mahata SK, Taupenot L, Rozansky DJ, Parmer RJ, O'Connor DT. Stimulus-transcription coupling in pheochromocytoma cells. Promoter region-specific activation of chromogranin A biosynthesis. J Biol Chem. 271:1996;28382-28390.
    • (1996) J Biol Chem , vol.271 , pp. 28382-28390
    • Tang, K.1    Wu, H.2    Mahata, S.K.3    Taupenot, L.4    Rozansky, D.J.5    Parmer, R.J.6    O'Connor, D.T.7
  • 26
    • 0031037662 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptor-mediated induction of zif268 mRNA in PC12D cells requires protein kinase C and the influx of extracellular calcium
    • Ebihara T, Saffen D. Muscarinic acetylcholine receptor-mediated induction of zif268 mRNA in PC12D cells requires protein kinase C and the influx of extracellular calcium. J Neurochem. 68:1997;1001-1010.
    • (1997) J Neurochem , vol.68 , pp. 1001-1010
    • Ebihara, T.1    Saffen, D.2
  • 29
    • 0028848552 scopus 로고
    • Regulated expression of the neural cell adhesion molecule L1 by specific patterns of neural impulses
    • Itoh K, Stevens B, Schachner M, Fields RD. Regulated expression of the neural cell adhesion molecule L1 by specific patterns of neural impulses. Science. 270:1995;1369-1372.
    • (1995) Science , vol.270 , pp. 1369-1372
    • Itoh, K.1    Stevens, B.2    Schachner, M.3    Fields, R.D.4
  • 30
    • 15844417346 scopus 로고    scopus 로고
    • Neuronal activity increases the phosphorylation of the transcription factor cAMP response element-binding protein (CREB) in rat hippocampus and cortex
    • Moore AN, Waxham MN, Dash PK. Neuronal activity increases the phosphorylation of the transcription factor cAMP response element-binding protein (CREB) in rat hippocampus and cortex. J Biol Chem. 271:1996;14214-14220.
    • (1996) J Biol Chem , vol.271 , pp. 14214-14220
    • Moore, A.N.1    Waxham, M.N.2    Dash, P.K.3
  • 31
    • 0027215902 scopus 로고
    • Regulation of gene expression in hippocampal neurons by distinct calcium signaling pathways
    • Bading H, Ginty DD, Greenberg ME. Regulation of gene expression in hippocampal neurons by distinct calcium signaling pathways. Science. 260:1993;181-186.
    • (1993) Science , vol.260 , pp. 181-186
    • Bading, H.1    Ginty, D.D.2    Greenberg, M.E.3
  • 32
    • 0028983401 scopus 로고
    • N-methyl-D-aspartate receptors activate transcription of c-fos and NGFI-A by distinct phospholipase A2-requiring intracellular signaling pathways
    • Lerea LS, Carlson NG, McNamara JO. N-methyl-D-aspartate receptors activate transcription of c-fos and NGFI-A by distinct phospholipase A2-requiring intracellular signaling pathways. Mol Pharmacol. 47:1995;1119-1125.
    • (1995) Mol Pharmacol , vol.47 , pp. 1119-1125
    • Lerea, L.S.1    Carlson, N.G.2    McNamara, J.O.3
  • 33
    • 0028921367 scopus 로고
    • Dopaminergic regulation of transcription factor expression in organotypic cultures of developing striatum
    • Liu FC, Takahashi H, McKay RD, Graybiel AM. Dopaminergic regulation of transcription factor expression in organotypic cultures of developing striatum. J Neurosci. 15:1995;2367-2384.
    • (1995) J Neurosci , vol.15 , pp. 2367-2384
    • Liu, F.C.1    Takahashi, H.2    McKay, R.D.3    Graybiel, A.M.4
  • 34
    • 0030463470 scopus 로고    scopus 로고
    • 2+- And stimulus duration-dependent switch for hippocampal gene expression
    • Prolonged, but not transient, CREB phosphorylation is required for CRE-regulated gene induction. The phosphorylation state of CREB is activated by a CaMKK - CaMKIV cascade, while a negative regulation is mediated by PP1 activity, regulated by a cytoplasmic calcineurin. Prolonged synaptic stimulation induces activity-induced inactivation of calcineurin, and slows the rate of pCREB dephosphorylation, thus allowing synaptic-activity-induced CRE activation. of outstanding interest
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression. Cell. 87:1996;1203-1214 Prolonged, but not transient, CREB phosphorylation is required for CRE-regulated gene induction. The phosphorylation state of CREB is activated by a CaMKK - CaMKIV cascade, while a negative regulation is mediated by PP1 activity, regulated by a cytoplasmic calcineurin. Prolonged synaptic stimulation induces activity-induced inactivation of calcineurin, and slows the rate of pCREB dephosphorylation, thus allowing synaptic-activity-induced CRE activation. of outstanding interest.
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 35
    • 0030452360 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of CREB phosphorylation: Transient versus sustained phosphorylation in the developing striatum
    • In an organotypic striatal slice preparation, sustained, but not transient, CREB phosphorylation was found to be critical in c-fos induction. Transience of CREB phosphorylation was regulated by a calcineurin-controlled phosphatase gate in striosomal neurons (DARPP-32-positive) but not in matrix neurons (DARPP-32-negative). of outstanding interest
    • Liu FC, Graybiel AM. Spatiotemporal dynamics of CREB phosphorylation: transient versus sustained phosphorylation in the developing striatum. Neuron. 17:1996;1133-1144 In an organotypic striatal slice preparation, sustained, but not transient, CREB phosphorylation was found to be critical in c-fos induction. Transience of CREB phosphorylation was regulated by a calcineurin-controlled phosphatase gate in striosomal neurons (DARPP-32-positive) but not in matrix neurons (DARPP-32-negative). of outstanding interest.
    • (1996) Neuron , vol.17 , pp. 1133-1144
    • Liu, F.C.1    Graybiel, A.M.2
  • 36
    • 0029887156 scopus 로고    scopus 로고
    • Gene expression of the transcription factor NF-kappa B in hippocampus: Regulation by synaptic activity
    • Meberg PJ, Kinney WR, Valcourt EG, Routtenberg A. Gene expression of the transcription factor NF-kappa B in hippocampus: regulation by synaptic activity. Mol Brain Res. 38:1996;179-190.
    • (1996) Mol Brain Res , vol.38 , pp. 179-190
    • Meberg, P.J.1    Kinney, W.R.2    Valcourt, E.G.3    Routtenberg, A.4
  • 37
    • 0029328342 scopus 로고
    • Transcriptional control by protein phosphorylation: Signal transmission from the cell surface to the nucleus
    • Karin M, Hunter T. Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus. Curr Biol. 5:1995;747-757.
    • (1995) Curr Biol , vol.5 , pp. 747-757
    • Karin, M.1    Hunter, T.2
  • 38
    • 0029693897 scopus 로고    scopus 로고
    • The JAK-STAT pathway: Summary of initial studies and recent advances
    • Darnell JE Jr. The JAK-STAT pathway: summary of initial studies and recent advances. Recent Prog Horm Res. 51:1996;391-403.
    • (1996) Recent Prog Horm Res , vol.51 , pp. 391-403
    • Darnell J.E., Jr.1
  • 39
    • 0029564149 scopus 로고
    • Transcription factors responsive to cAMP
    • Sassone-Corsi P. Transcription factors responsive to cAMP. Annu Rev Cell Dev Biol. 11:1995;355-377.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 355-377
    • Sassone-Corsi, P.1
  • 40
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • in press
    • Montminy MR. Transcriptional regulation by cyclic AMP. Annu Rev Biochem. 66:1997;. in press.
    • (1997) Annu Rev Biochem , vol.66
    • Montminy, M.R.1
  • 42
    • 0027981633 scopus 로고
    • Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression
    • Matthews RP, Guthrie CR, Wailes LM, Zhao X, Means AR, McKnight GS. Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression. Mol Cell Biol. 14:1994;6107-6116.
    • (1994) Mol Cell Biol , vol.14 , pp. 6107-6116
    • Matthews, R.P.1    Guthrie, C.R.2    Wailes, L.M.3    Zhao, X.4    Means, A.R.5    McKnight, G.S.6
  • 43
    • 0027943988 scopus 로고
    • 2+/calmodulin-dependent protein kinase type II and type IV involves phosphorylation of a site that negatively regulates activity
    • 2+/calmodulin-dependent protein kinase type II and type IV involves phosphorylation of a site that negatively regulates activity. Genes Dev. 8:1994;2527-2539.
    • (1994) Genes Dev , vol.8 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 44
    • 0028338460 scopus 로고
    • Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Ginty DD, Bonni A, Greenberg ME. Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell. 77:1994;713-725.
    • (1994) Cell , vol.77 , pp. 713-725
    • Ginty, D.D.1    Bonni, A.2    Greenberg, M.E.3
  • 46
    • 0028925179 scopus 로고
    • Phosphorylation of CREB by CaM-kinase IV activated by CaM-kinase IV kinase
    • Enslen H, Tokumitsu H, Soderling TR. Phosphorylation of CREB by CaM-kinase IV activated by CaM-kinase IV kinase. Biochem Biophys Res Commun. 207:1995;1038-1043.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 1038-1043
    • Enslen, H.1    Tokumitsu, H.2    Soderling, T.R.3
  • 47
    • 0029057392 scopus 로고
    • Transcriptional activation of egr-1 by granulocyte-macrophage colony-stimulating factor but not interleukin 3 requires phosphorylation of cAMP response element-binding protein (CREB) on serine 133
    • Lee HJ, Mignacca RC, Sakamoto KM. Transcriptional activation of egr-1 by granulocyte-macrophage colony-stimulating factor but not interleukin 3 requires phosphorylation of cAMP response element-binding protein (CREB) on serine 133. J Biol Chem. 270:1995;15979-15983.
    • (1995) J Biol Chem , vol.270 , pp. 15979-15983
    • Lee, H.J.1    Mignacca, R.C.2    Sakamoto, K.M.3
  • 48
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • By fractionating a growth-factor-stimulated CREB phosphorylating activity, a CREB kinase was purified and identified as rsk-2. Dominant-negative rsk-2-abolished growth-factor-mediated CRE activation, thus highlighting the critical importance of a Ras/MAPK/rsk-2 pathway upstream of CREB phosphorylation during a growth-factor-dependent process. of special interest
    • Xing J, Ginty DD, Greenberg ME. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science. 273:1996;959-963 By fractionating a growth-factor-stimulated CREB phosphorylating activity, a CREB kinase was purified and identified as rsk-2. Dominant-negative rsk-2-abolished growth-factor-mediated CRE activation, thus highlighting the critical importance of a Ras/MAPK/rsk-2 pathway upstream of CREB phosphorylation during a growth-factor-dependent process. of special interest.
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 49
    • 0029790656 scopus 로고    scopus 로고
    • FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2
    • Tan Y, Rouse J, Zhang A, Cariati S, Cohen P, Comb MJ. FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. EMBO J. 15:1996;4629-4642.
    • (1996) EMBO J , vol.15 , pp. 4629-4642
    • Tan, Y.1    Rouse, J.2    Zhang, A.3    Cariati, S.4    Cohen, P.5    Comb, M.J.6
  • 50
    • 0030207894 scopus 로고    scopus 로고
    • Versatile molecular glue. Transcriptional control
    • Janknecht R, Hunter T. Versatile molecular glue. Transcriptional control. Curr Biol. 6:1996;951-954.
    • (1996) Curr Biol , vol.6 , pp. 951-954
    • Janknecht, R.1    Hunter, T.2
  • 51
    • 0029991520 scopus 로고    scopus 로고
    • Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP
    • Janknecht R, Nordheim A. Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP. Oncogene. 12:1996;1961-1969.
    • (1996) Oncogene , vol.12 , pp. 1961-1969
    • Janknecht, R.1    Nordheim, A.2
  • 52
    • 0030029419 scopus 로고    scopus 로고
    • Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator
    • Kee BI, Arias J, Montminy MR. Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator. J Biol Chem. 271:1996;2373-2375.
    • (1996) J Biol Chem , vol.271 , pp. 2373-2375
    • Kee, B.I.1    Arias, J.2    Montminy, M.R.3
  • 53
    • 0030597282 scopus 로고    scopus 로고
    • MAP kinase-dependent transcriptional coactivation of Elk-1 and its cofactor CBP
    • Janknecht R, Nordheim A. MAP kinase-dependent transcriptional coactivation of Elk-1 and its cofactor CBP. Biochem Biophys Res Commun. 228:1996;831-837.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 831-837
    • Janknecht, R.1    Nordheim, A.2
  • 54
    • 0029904571 scopus 로고    scopus 로고
    • CREB-binding protein activates transcription through multiple domains
    • Association of a PKA-sensitive factor to the amino-terminal portion of CBP is sufficient to provide full CBP activation. of special interest
    • Swope DL, Mueller CL, Chrivia JC. CREB-binding protein activates transcription through multiple domains. J Biol Chem. 271:1996;28138-28145 Association of a PKA-sensitive factor to the amino-terminal portion of CBP is sufficient to provide full CBP activation. of special interest.
    • (1996) J Biol Chem , vol.271 , pp. 28138-28145
    • Swope, D.L.1    Mueller, C.L.2    Chrivia, J.C.3
  • 55
    • 0000631273 scopus 로고    scopus 로고
    • The signal-dependent coactivator CBP is a nuclear target for pp90RSK
    • Whereas binding of pp90rsk inhibits CREB-mediated gene induction, it is required for Ras-mediated gene expression. of special interest
    • Nakajima T, Fukamizu A, Takahashi J, Gage FH, Fisher T, Blenis J, Montminy MR. The signal-dependent coactivator CBP is a nuclear target for pp90RSK. Cell. 86:1996;465-474 Whereas binding of pp90rsk inhibits CREB-mediated gene induction, it is required for Ras-mediated gene expression. of special interest.
    • (1996) Cell , vol.86 , pp. 465-474
    • Nakajima, T.1    Fukamizu, A.2    Takahashi, J.3    Gage, F.H.4    Fisher, T.5    Blenis, J.6    Montminy, M.R.7
  • 56
    • 0030570961 scopus 로고    scopus 로고
    • Transcription: A growing coactivator network
    • Janknecht R, Hunter T. Transcription: a growing coactivator network. Nature. 383:1996;22-23.
    • (1996) Nature , vol.383 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 57
    • 0242587820 scopus 로고    scopus 로고
    • A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
    • See annotation [60]. of outstanding interest
    • Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin SC, Heyman RA, Rose DW, Glass CK, Rosenfeld MG. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell. 85:1996;403-414 See annotation [60]. of outstanding interest.
    • (1996) Cell , vol.85 , pp. 403-414
    • Kamei, Y.1    Xu, L.2    Heinzel, T.3    Torchia, J.4    Kurokawa, R.5    Gloss, B.6    Lin, S.C.7    Heyman, R.A.8    Rose, D.W.9    Glass, C.K.10    Rosenfeld, M.G.11
  • 59
    • 0029767462 scopus 로고    scopus 로고
    • Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha
    • See annotation [60]. of outstanding interest
    • Bhattacharya S, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, Livingston DM. Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. Nature. 383:1996;344-347 See annotation [60]. of outstanding interest.
    • (1996) Nature , vol.383 , pp. 344-347
    • Bhattacharya, S.1    Eckner, R.2    Grossman, S.3    Oldread, E.4    Arany, Z.5    D'Andrea, A.6    Livingston, D.M.7
  • 60
    • 0029875008 scopus 로고    scopus 로고
    • Control of cAMP-regulated enhancers by the viral transactivator Tax through CREB and the co-activator CBP
    • These papers [57-60,61-70] illustrate how many transcription factors can bind CBP and modify its transactivation potential, providing a convenient point of convergence downstream of a wide variety of signaling pathways. of outstanding interest
    • Kwok RP, Laurance ME, Lundblad JR, Goldman PS, Shih H, Connor LM, Marriott SJ, Goodman RH. Control of cAMP-regulated enhancers by the viral transactivator Tax through CREB and the co-activator CBP. Nature. 380:1996;642-646 These papers [57-60,61-70] illustrate how many transcription factors can bind CBP and modify its transactivation potential, providing a convenient point of convergence downstream of a wide variety of signaling pathways. of outstanding interest.
    • (1996) Nature , vol.380 , pp. 642-646
    • Kwok, R.P.1    Laurance, M.E.2    Lundblad, J.R.3    Goldman, P.S.4    Shih, H.5    Connor, L.M.6    Marriott, S.J.7    Goodman, R.H.8
  • 63
    • 0029825698 scopus 로고    scopus 로고
    • Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation
    • Eckner R, Yao TP, Oldread E, Livingston DM. Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation. Genes Dev. 10:1996;2478-2490.
    • (1996) Genes Dev , vol.10 , pp. 2478-2490
    • Eckner, R.1    Yao, T.P.2    Oldread, E.3    Livingston, D.M.4
  • 64
    • 0029786690 scopus 로고    scopus 로고
    • CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription
    • Smith CL, Onate SA, Tsai MJ, O'Malley BW. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc Natl Acad Sci USA. 93:1996;8884-8888.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8884-8888
    • Smith, C.L.1    Onate, S.A.2    Tsai, M.J.3    O'Malley, B.W.4
  • 65
    • 0029939490 scopus 로고    scopus 로고
    • Differential interactions of the CREB/ATF family of transcription factors with p300 and adenovirus E1A
    • Lee JS, Zhang X, Shi Y. Differential interactions of the CREB/ATF family of transcription factors with p300 and adenovirus E1A. J Biol Chem. 271:1996;17666-17674.
    • (1996) J Biol Chem , vol.271 , pp. 17666-17674
    • Lee, J.S.1    Zhang, X.2    Shi, Y.3
  • 66
    • 0029968939 scopus 로고    scopus 로고
    • Human p300 protein is a coactivator for the transcription factor MyoD
    • Yuan W, Condorelli G, Caruso M, Felsani A, Giordano A. Human p300 protein is a coactivator for the transcription factor MyoD. J Biol Chem. 271:1996;9009-9013.
    • (1996) J Biol Chem , vol.271 , pp. 9009-9013
    • Yuan, W.1    Condorelli, G.2    Caruso, M.3    Felsani, A.4    Giordano, A.5
  • 67
    • 10544235694 scopus 로고    scopus 로고
    • SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein
    • Oliner JD, Andresen JM, Hansen SK, Zhou S, Tjian R. SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein. Genes Dev. 10:1996;2903-2911.
    • (1996) Genes Dev , vol.10 , pp. 2903-2911
    • Oliner, J.D.1    Andresen, J.M.2    Hansen, S.K.3    Zhou, S.4    Tjian, R.5
  • 70
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins ND, Felzien LK, Betts JC, Leung K, Beach DH, Nabel GJ. Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator. Science. 275:1997;523-527.
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 71
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 382:1996;319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 72
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • See annotation [73]. of outstanding interest
    • Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature. 384:1996;641-643 See annotation [73]. of outstanding interest.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 73
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • These two papers [72,73] demonstrate that CBP is a histone acetyltransferase. of outstanding interest
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959 These two papers [72,73] demonstrate that CBP is a histone acetyltransferase. of outstanding interest.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 74
    • 0029133577 scopus 로고
    • A molecular switch for the consolidation of long-term memory: CAMP-inducible gene expression
    • Alberini CM, Ghirardi M, Huang YY, Nguyen PV, Kandel ER. A molecular switch for the consolidation of long-term memory: cAMP-inducible gene expression. Ann NY Acad Sci. 758:1995;261-286.
    • (1995) Ann NY Acad Sci , vol.758 , pp. 261-286
    • Alberini, C.M.1    Ghirardi, M.2    Huang, Y.Y.3    Nguyen, P.V.4    Kandel, E.R.5
  • 76
    • 0030021048 scopus 로고    scopus 로고
    • Molecular enhancement of memory formation
    • Carew TJ. Molecular enhancement of memory formation. Neuron. 16:1996;5-8.
    • (1996) Neuron , vol.16 , pp. 5-8
    • Carew, T.J.1
  • 77
    • 0029561823 scopus 로고
    • Aplysia CREB2 represses long-term facilitation: Relief of repression converts transient facilitation into long-term functional and structural change
    • dCREB2, an inhibitory isoform of the CREB gene, is identified as binding partner of ApC/EBP. Over-expression of dCREB2 suppresses long-term sensitization and abolishes activity-induced increases in varicosities in Aplysia sensory neurons. of outstanding interest
    • Bartsch D, Ghirardi M, Skehel PA, Karl KA, Herder SP, Chen M, Bailey CH, Kandel ER. Aplysia CREB2 represses long-term facilitation: relief of repression converts transient facilitation into long-term functional and structural change. Cell. 1995; dCREB2, an inhibitory isoform of the CREB gene, is identified as binding partner of ApC/EBP. Over-expression of dCREB2 suppresses long-term sensitization and abolishes activity-induced increases in varicosities in Aplysia sensory neurons. of outstanding interest.
    • (1995) Cell
    • Bartsch, D.1    Ghirardi, M.2    Skehel, P.A.3    Karl, K.A.4    Herder, S.P.5    Chen, M.6    Bailey, C.H.7    Kandel, E.R.8
  • 78
    • 0027983479 scopus 로고
    • Induction of a dominant negative CREB transgene specifically blocks long-term memory in Drosophila
    • Yin JC, Wallach JS, Del Vecchio M, Wilder EL, Zhou H, Quinn WG, Tully T. Induction of a dominant negative CREB transgene specifically blocks long-term memory in Drosophila. Cell. 79:1994;49-58.
    • (1994) Cell , vol.79 , pp. 49-58
    • Yin, J.C.1    Wallach, J.S.2    Del Vecchio, M.3    Wilder, E.L.4    Zhou, H.5    Quinn, W.G.6    Tully, T.7
  • 79
    • 0028934097 scopus 로고
    • CREB as a memory modulator: Induced expression of a dCREB2 activator isoform enhances long-term memory in Drosophila
    • Yin JC, Del Vecchio M, Zhou H, Tully T. CREB as a memory modulator: induced expression of a dCREB2 activator isoform enhances long-term memory in Drosophila. Cell. 81:1995;107-115.
    • (1995) Cell , vol.81 , pp. 107-115
    • Yin, J.C.1    Del Vecchio, M.2    Zhou, H.3    Tully, T.4
  • 80
    • 0029950182 scopus 로고    scopus 로고
    • CREB and the formation of long-term memory
    • A model is presented in which the balance between CREB activators and CREB inhibitors is critical in determining the amount of effective downstream transcriptional activation. of outstanding interest
    • Yin JC, Tully T. CREB and the formation of long-term memory. Curr Opin Neurobiol. 6:1996;264-268 A model is presented in which the balance between CREB activators and CREB inhibitors is critical in determining the amount of effective downstream transcriptional activation. of outstanding interest.
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 264-268
    • Yin, J.C.1    Tully, T.2
  • 81
    • 0028071507 scopus 로고
    • Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein
    • Bourtchuladze R, Frenguelli B, Blendy J, Cioffi D, Schutz G, Silva AJ. Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein. Cell. 79:1994;59-68.
    • (1994) Cell , vol.79 , pp. 59-68
    • Bourtchuladze, R.1    Frenguelli, B.2    Blendy, J.3    Cioffi, D.4    Schutz, G.5    Silva, A.J.6
  • 82
    • 0031027626 scopus 로고    scopus 로고
    • Spaced training induces normal long-term memory in CREB mutant mice
    • In CREBα/δ-homozygous knockout mice, long-term memory associated with hippocampal function is significantly deficient relative to wild-type mice in three independent learning paradigms (contextual fear conditioning, Morris water maze, social transmission of food preference). However, this defect can be rescued if a second trial is provided with an intertrial interval of one hour, but not one minute, indicating the critical importance of timing. of outstanding interest
    • Kogan JH, Frankland PW, Blendy JA, Coblentz J, Marowitz Z, Schutz G, Silva AJ. Spaced training induces normal long-term memory in CREB mutant mice. Curr Biol. 7:1997;1-11 In CREBα/δ-homozygous knockout mice, long-term memory associated with hippocampal function is significantly deficient relative to wild-type mice in three independent learning paradigms (contextual fear conditioning, Morris water maze, social transmission of food preference). However, this defect can be rescued if a second trial is provided with an intertrial interval of one hour, but not one minute, indicating the critical importance of timing. of outstanding interest.
    • (1997) Curr Biol , vol.7 , pp. 1-11
    • Kogan, J.H.1    Frankland, P.W.2    Blendy, J.A.3    Coblentz, J.4    Marowitz, Z.5    Schutz, G.6    Silva, A.J.7
  • 83
    • 0029812609 scopus 로고    scopus 로고
    • Luteinizing hormone deficiency and female infertility in mice lacking the transcription factor NGFI-A (Egr-1)
    • Lee SL, Sadovsky Y, Swirnoff AH, Polish JA, Goda P, Gavrilina G, Milbrandt J. Luteinizing hormone deficiency and female infertility in mice lacking the transcription factor NGFI-A (Egr-1). Science. 273:1996;1219-1221.
    • (1996) Science , vol.273 , pp. 1219-1221
    • Lee, S.L.1    Sadovsky, Y.2    Swirnoff, A.H.3    Polish, J.A.4    Goda, P.5    Gavrilina, G.6    Milbrandt, J.7
  • 86
    • 0030602817 scopus 로고    scopus 로고
    • A defect in nurturing in mice lacking the immediate early gene fosB
    • Brown JR, Ye H, Bronson RT, Dikkes P, Greenberg ME. A defect in nurturing in mice lacking the immediate early gene fosB. Cell. 86:1996;297-309.
    • (1996) Cell , vol.86 , pp. 297-309
    • Brown, J.R.1    Ye, H.2    Bronson, R.T.3    Dikkes, P.4    Greenberg, M.E.5
  • 87
    • 0030952362 scopus 로고    scopus 로고
    • Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory
    • Abel T, Nguyen PV, Barad M, Deuel TAS, Kandel ER, Bourtchouladze R. Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory. Cell. 88:1997;615-626.
    • (1997) Cell , vol.88 , pp. 615-626
    • Abel, T.1    Nguyen, P.V.2    Barad, M.3    Deuel, T.A.S.4    Kandel, E.R.5    Bourtchouladze, R.6
  • 88
    • 0027166104 scopus 로고
    • Coupling of hormonal stimulation and transcription via the cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase A
    • Hagiwara M, Brindle P, Harootunian A, Armstrong R, Rivier J, Vale W, Tsien R, Montminy MR. Coupling of hormonal stimulation and transcription via the cyclic AMP-responsive factor CREB is rate limited by nuclear entry of protein kinase A. Mol Cell Biol. 13:1993;4852-4859.
    • (1993) Mol Cell Biol , vol.13 , pp. 4852-4859
    • Hagiwara, M.1    Brindle, P.2    Harootunian, A.3    Armstrong, R.4    Rivier, J.5    Vale, W.6    Tsien, R.7    Montminy, M.R.8
  • 89
    • 0027991139 scopus 로고
    • Induction of c-fos expression in hypothalamic magnocellular neurons requires synaptic activation and not simply increased spike activity
    • Luckman SM, Dyball RE, Leng G. Induction of c-fos expression in hypothalamic magnocellular neurons requires synaptic activation and not simply increased spike activity. J Neurosci. 14:1994;4825-4830.
    • (1994) J Neurosci , vol.14 , pp. 4825-4830
    • Luckman, S.M.1    Dyball, R.E.2    Leng, G.3
  • 90
    • 0027164611 scopus 로고
    • Requirement of brain extract for the activity of brain calmodulin-dependent protein kinase IV expressed in Escherichia coli
    • Okuno S, Fujisawa H. Requirement of brain extract for the activity of brain calmodulin-dependent protein kinase IV expressed in Escherichia coli. J Biochem. 114:1993;167-170.
    • (1993) J Biochem , vol.114 , pp. 167-170
    • Okuno, S.1    Fujisawa, H.2
  • 92
    • 0027947119 scopus 로고
    • 2+-calmodulin-dependent protein kinase la
    • 2+-calmodulin-dependent protein kinase la. J Biol Chem. 269:1994;2158-2164.
    • (1994) J Biol Chem , vol.269 , pp. 2158-2164
    • Lee, J.C.1    Edelman, A.M.2
  • 94
    • 0028171361 scopus 로고
    • 2+/calmodulin-dependent protein kinase IV kinase from rat brain
    • 2+/calmodulin-dependent protein kinase IV kinase from rat brain. J Biochem. 116:1994;923-930.
    • (1994) J Biochem , vol.116 , pp. 923-930
    • Okuno, S.1    Kitani, T.2    Fujisawa, H.3
  • 96
    • 0029786417 scopus 로고    scopus 로고
    • Activation of a calcium-calmodulin-dependent protein kinase I cascade in PC12 cells
    • Aletta JM, Selbert MA, Nairn AC, Edelman AM. Activation of a calcium-calmodulin-dependent protein kinase I cascade in PC12 cells. J Biol Chem. 271:1996;20930-20934.
    • (1996) J Biol Chem , vol.271 , pp. 20930-20934
    • Aletta, J.M.1    Selbert, M.A.2    Nairn, A.C.3    Edelman, A.M.4
  • 97
    • 0028978850 scopus 로고
    • 2+/calmodulin-dependent protein kinase cascade. Molecular cloning and expression of calcium/calmodulin-dependent protein kinase kinase
    • Molecular cloning of CaMKK demonstrated that it is a member of the CaMK gene family. Coexpression of CaMKK with either CaMKIV or CaMKI dramatically increase CRE-dependent transcription. of outstanding interest
    • 2+/calmodulin-dependent protein kinase cascade. Molecular cloning and expression of calcium/calmodulin-dependent protein kinase kinase. J Biol Chem. 270:1995;19320-19324 Molecular cloning of CaMKK demonstrated that it is a member of the CaMK gene family. Coexpression of CaMKK with either CaMKIV or CaMKI dramatically increase CRE-dependent transcription. of outstanding interest.
    • (1995) J Biol Chem , vol.270 , pp. 19320-19324
    • Tokumitsu, H.1    Enslen, H.2    Soderling, T.R.3
  • 98
    • 0028890090 scopus 로고
    • Preparation and characterization of calmodulin-dependent protein kinase IV (CaM-kinase IV) free of CaM-kinase IV kinase from rat cerebral cortex
    • Kameshita I, Fujisawa H. Preparation and characterization of calmodulin-dependent protein kinase IV (CaM-kinase IV) free of CaM-kinase IV kinase from rat cerebral cortex. J Biochem. 117:1995;85-90.
    • (1995) J Biochem , vol.117 , pp. 85-90
    • Kameshita, I.1    Fujisawa, H.2
  • 99
    • 0029125761 scopus 로고
    • Human calcium-calmodulin dependent protein kinase I: CDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase
    • Haribabu B, Hook S, Selbert MA, Goldstein EG, Tomhave ED, Edelman AM, Snyderman R, Means AR. Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. EMBO J. 14:1995;3679-3686.
    • (1995) EMBO J , vol.14 , pp. 3679-3686
    • Haribabu, B.1    Hook, S.2    Selbert, M.A.3    Goldstein, E.G.4    Tomhave, E.D.5    Edelman, A.M.6    Snyderman, R.7    Means, A.R.8
  • 102
    • 0030008563 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase IV kinase isoforms in rat brain
    • 2+/calmodulin-dependent protein kinase IV kinase isoforms in rat brain. J Biochem. 119:1996;1176-1181.
    • (1996) J Biochem , vol.119 , pp. 1176-1181
    • Okuno, S.1    Kitani, T.2    Fujisawa, H.3
  • 103
    • 0030637371 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase kinase β from rat cerebellum
    • Another CaMKK isoform was found in the cerebellum, a preferred site for CaMKIV expression, suggesting a certain degree of tissue-specific regulation of the CaMKK cascade by differential expression of CaMKK isoforms. of special interest
    • 2+/calmodulin-dependent protein kinase kinase β from rat cerebellum. J Biochem. 121:1997;155-160 Another CaMKK isoform was found in the cerebellum, a preferred site for CaMKIV expression, suggesting a certain degree of tissue-specific regulation of the CaMKK cascade by differential expression of CaMKK isoforms. of special interest.
    • (1997) J Biochem , vol.121 , pp. 155-160
    • Okuno, S.1    Kitani, T.2    Fujisawa, H.3
  • 104
    • 0030044258 scopus 로고    scopus 로고
    • Fine tuning of calcium entry into neurons regulates adenosine 3′,5′-monophoshate-dependent transcription by several distinct mechanisms
    • Barthel F, Boutillier AL, Trouslard J, Loeffler JP. Fine tuning of calcium entry into neurons regulates adenosine 3′,5′-monophoshate-dependent transcription by several distinct mechanisms. Neuroscience. 70:1996;1053-1065.
    • (1996) Neuroscience , vol.70 , pp. 1053-1065
    • Barthel, F.1    Boutillier, A.L.2    Trouslard, J.3    Loeffler, J.P.4
  • 105
    • 0028916490 scopus 로고
    • Phosphorylation of DARPP-32, a dopamine- And cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo
    • Desdouits F, Cohen D, Nairn AC, Greengard P, Girault JA. Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo. J Biol Chem. 270:1995;8772-8778.
    • (1995) J Biol Chem , vol.270 , pp. 8772-8778
    • Desdouits, F.1    Cohen, D.2    Nairn, A.C.3    Greengard, P.4    Girault, J.A.5
  • 106
    • 0029851279 scopus 로고    scopus 로고
    • Regulation of type I adenylyl cyclase by calmodulin kinase IV in vivo
    • See annotation [113]. of special interest
    • Wayman GA, Wei J, Wong S, Storm DR. Regulation of type I adenylyl cyclase by calmodulin kinase IV in vivo. Mol Cell Biol. 16:1996;6075-6082 See annotation [113]. of special interest.
    • (1996) Mol Cell Biol , vol.16 , pp. 6075-6082
    • Wayman, G.A.1    Wei, J.2    Wong, S.3    Storm, D.R.4
  • 107
    • 0030032998 scopus 로고    scopus 로고
    • Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels
    • Rosen LB, Greenberg ME. Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels. Proc Natl Acad Sci USA. 93:1996;1113-1118.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1113-1118
    • Rosen, L.B.1    Greenberg, M.E.2
  • 108
    • 0029800074 scopus 로고    scopus 로고
    • Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism
    • NMDA-mediated SRE activation in hippocampal neurons was blocked by overexpression of dominant-negative Ras and dominant-negative ERK. of special interest
    • Xia Z, Dudek H, Miranti CK, Greenberg ME. Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism. J Neurosci. 16:1996;5425-5436 NMDA-mediated SRE activation in hippocampal neurons was blocked by overexpression of dominant-negative Ras and dominant-negative ERK. of special interest.
    • (1996) J Neurosci , vol.16 , pp. 5425-5436
    • Xia, Z.1    Dudek, H.2    Miranti, C.K.3    Greenberg, M.E.4
  • 109
    • 0031034108 scopus 로고    scopus 로고
    • Neurotransmitter- And growth factor-induced cAMP response element binding protein phosphorylation in glial cell progenitors: Role of calcium ions, protein kinase C, and mitogen-activated protein kinase/ribosomal S6 kinase pathway
    • Pende M, Fisher TL, Simpson PB, Russell JT, Blenis J, Gallo V. Neurotransmitter- and growth factor-induced cAMP response element binding protein phosphorylation in glial cell progenitors: role of calcium ions, protein kinase C, and mitogen-activated protein kinase/ribosomal S6 kinase pathway. J Neurosci. 17:1997;1291-1301.
    • (1997) J Neurosci , vol.17 , pp. 1291-1301
    • Pende, M.1    Fisher, T.L.2    Simpson, P.B.3    Russell, J.T.4    Blenis, J.5    Gallo, V.6
  • 111
    • 0029742101 scopus 로고    scopus 로고
    • The N-terminal pleckstrin, coiled-coil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium
    • 2+-dependent activation of Ras-GRF. of outstanding interest
    • 2+-dependent activation of Ras-GRF. of outstanding interest.
    • (1996) Mol Cell Biol , vol.16 , pp. 4888-4896
    • Buchsbaum, R.1    Telliez, J.B.2    Goonesekera, S.3    Feig, L.A.4
  • 113
    • 0029768088 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade
    • Two recent papers [106,113] have provided examples of crosstalk between various activity-dependent signal cascades. Wayman et al. [106] showed adenylyl cyclase type I is inhibited upon specific phosphorylation by CaMKIV but not CaMKII. In their paper, Enslen et al. [113] provide evidence for an interplay between CaMKs and MAPKs: overexpression of activated forms of CaMKIV and CaMKK increased substantially the basal activity of MAPKs (ERK1, ERK2, JNK1, and p38) and SRE-dependent transcription. Furthermore, Wayman et al. (GA Wayman, H Tokumitsu, TR Soderling, Soc Neurosci Abstr 1996, 22:372) suggest that PKA-induced phosphorylation of CaMKKα inhibits its activity towards CaMKIV. of special interest
    • Enslen H, Tokumitsu H, Stork PJ, Davis RJ, Soderling TR. Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade. Proc Natl Acad Sci USA. 93:1996;10803-10808 Two recent papers [106,113] have provided examples of crosstalk between various activity-dependent signal cascades. Wayman et al. [106] showed adenylyl cyclase type I is inhibited upon specific phosphorylation by CaMKIV but not CaMKII. In their paper, Enslen et al. [113] provide evidence for an interplay between CaMKs and MAPKs: overexpression of activated forms of CaMKIV and CaMKK increased substantially the basal activity of MAPKs (ERK1, ERK2, JNK1, and p38) and SRE-dependent transcription. Furthermore, Wayman et al. (GA Wayman, H Tokumitsu, TR Soderling, Soc Neurosci Abstr 1996, 22:372) suggest that PKA-induced phosphorylation of CaMKKα inhibits its activity towards CaMKIV. of special interest.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10803-10808
    • Enslen, H.1    Tokumitsu, H.2    Stork, P.J.3    Davis, R.J.4    Soderling, T.R.5
  • 114
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs
    • Hart MJ, Callow MG, Souza B, Polakis P. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs. EMBO J. 15:1996;2997-3005.
    • (1996) EMBO J , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 116
    • 0029784514 scopus 로고    scopus 로고
    • The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
    • Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ. The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol Cell Biol. 16:1996;4869-4878.
    • (1996) Mol Cell Biol , vol.16 , pp. 4869-4878
    • Brill, S.1    Li, S.2    Lyman, C.W.3    Church, D.M.4    Wasmuth, J.J.5    Weissbach, L.6    Bernards, A.7    Snijders, A.J.8
  • 117
    • 9544225039 scopus 로고    scopus 로고
    • Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAP1 and a Cdc42Hs binding partner with similarity to IQGAP2
    • McCallum SJ, Wu WJ, Cerione RA. Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAP1 and a Cdc42Hs binding partner with similarity to IQGAP2. J Biol Chem. 271:1996;21732-21327.
    • (1996) J Biol Chem , vol.271 , pp. 21732-21327
    • McCallum, S.J.1    Wu, W.J.2    Cerione, R.A.3
  • 118
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G, Dikic I, Lev S, 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
  • 119
    • 0028889203 scopus 로고
    • Regulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elements
    • Using transgenic lines carrying a few copies of the complete or mutated 5′-flanking region of the c-fos gene fused to a lacZ reporter, the cooperativity of various regulatory elements (e.g., SRE, SIE, FAP and CRE) is established. of outstanding interest
    • Robertson LM, Kerppola TK, Vendrell M, Luk D, Smeyne RJ, Bocchiaro C, Morgan JI, Curran T. Regulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elements. Neuron. 14:1995;241-252 Using transgenic lines carrying a few copies of the complete or mutated 5′-flanking region of the c-fos gene fused to a lacZ reporter, the cooperativity of various regulatory elements (e.g., SRE, SIE, FAP and CRE) is established. of outstanding interest.
    • (1995) Neuron , vol.14 , pp. 241-252
    • Robertson, L.M.1    Kerppola, T.K.2    Vendrell, M.3    Luk, D.4    Smeyne, R.J.5    Bocchiaro, C.6    Morgan, J.I.7    Curran, T.8
  • 120
    • 15844416253 scopus 로고    scopus 로고
    • Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity
    • See annotation [122]. of outstanding interest
    • Loh C, Shaw KT, Carew J, Viola JP, Luo C, Perrino BA, Rao A. Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity. J Biol Chem. 271:1996;10884-10891 See annotation [122]. of outstanding interest.
    • (1996) J Biol Chem , vol.271 , pp. 10884-10891
    • Loh, C.1    Shaw, K.T.2    Carew, J.3    Viola, J.P.4    Luo, C.5    Perrino, B.A.6    Rao, A.7
  • 121
    • 0029761681 scopus 로고    scopus 로고
    • Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4
    • See annotation [122]. of outstanding interest
    • Shibasaki F, Price ER, Milan D, McKeon F. Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4. Nature. 382:1996;370-373 See annotation [122]. of outstanding interest.
    • (1996) Nature , vol.382 , pp. 370-373
    • Shibasaki, F.1    Price, E.R.2    Milan, D.3    McKeon, F.4
  • 122
    • 0029851762 scopus 로고    scopus 로고
    • 2+ signals and immunosuppression
    • 2+ influx is terminated, NFAT is rapidly exported from the nucleus, presumably after rephosphorylation. of outstanding interest
    • 2+ influx is terminated, NFAT is rapidly exported from the nucleus, presumably after rephosphorylation. of outstanding interest.
    • (1996) Nature , vol.383 , pp. 837-840
    • Timmerman, L.A.1    Clipstone, N.A.2    Ho, S.N.3    Northrop, J.P.4    Crabtree, G.R.5
  • 125
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: Role in EGF receptor-mediated tyrosine phosphorylation
    • EGF-induced activation of gene expression is critically dependent on the activation of a tyrosine kinase cascade initially triggered by tyrosine phosphorylation of the EGF receptor molecule itself. The authors show that this event is preceded by an inactivation of a tyrosine phosphatase, which is mediated by hydrogen peroxide. of outstanding interest
    • Bae YS, Kang SW, Seo MS, Baines IC, Tekle E, Chock PB, Rhee SG. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem. 272:1997;217-221 EGF-induced activation of gene expression is critically dependent on the activation of a tyrosine kinase cascade initially triggered by tyrosine phosphorylation of the EGF receptor molecule itself. The authors show that this event is preceded by an inactivation of a tyrosine phosphatase, which is mediated by hydrogen peroxide. of outstanding interest.
    • (1997) J Biol Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 126
    • 0029742102 scopus 로고    scopus 로고
    • Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of STAT1
    • See annotation [128]. of special interest
    • Shuai K, Liao J, Song MM. Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of STAT1. Mol Cell Biol. 16:1996;4932-4941 See annotation [128]. of special interest.
    • (1996) Mol Cell Biol , vol.16 , pp. 4932-4941
    • Shuai, K.1    Liao, J.2    Song, M.M.3
  • 127
    • 0029972194 scopus 로고    scopus 로고
    • The rapid inactivation of nuclear tyrosine phosphorylated STAT1 depends upon a protein tyrosine phosphatase
    • These two papers [126,127] establish the involvement of a nuclear tyrosine phosphatase in the inactivation of STAT. of special interest
    • Haspel RL, Salditt-Georgieff M, Darnell JE Jr. The rapid inactivation of nuclear tyrosine phosphorylated STAT1 depends upon a protein tyrosine phosphatase. EMBO J. 15:1996;6262-6268 These two papers [126,127] establish the involvement of a nuclear tyrosine phosphatase in the inactivation of STAT. of special interest.
    • (1996) EMBO J , vol.15 , pp. 6262-6268
    • Haspel, R.L.1    Salditt-Georgieff, M.2    Darnell J.E., Jr.3
  • 128
    • 0030272962 scopus 로고    scopus 로고
    • Cell adhesion molecules, CREB, and the formation of new synaptic connections
    • Martin KC, Kandel ER. Cell adhesion molecules, CREB, and the formation of new synaptic connections. Neuron. 17:1996;567-570.
    • (1996) Neuron , vol.17 , pp. 567-570
    • Martin, K.C.1    Kandel, E.R.2
  • 129
    • 0026554563 scopus 로고
    • Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia
    • Mayford M, Barzilai A, Keller F, Schacher S, Kandel ER. Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia. Science. 256:1992;638-644.
    • (1992) Science , vol.256 , pp. 638-644
    • Mayford, M.1    Barzilai, A.2    Keller, F.3    Schacher, S.4    Kandel, E.R.5
  • 130
    • 0026569052 scopus 로고
    • Serotonin-mediated endocytosis of apCAM: An early step of learning-related synaptic growth in Aplysia
    • Bailey CH, Chen M, Keller F, Kandel ER. Serotonin-mediated endocytosis of apCAM: an early step of learning-related synaptic growth in Aplysia. Science. 256:1992;645-649.
    • (1992) Science , vol.256 , pp. 645-649
    • Bailey, C.H.1    Chen, M.2    Keller, F.3    Kandel, E.R.4
  • 131
    • 0028230594 scopus 로고
    • Increase in extracellular NCAM and amyloid precursor protein following induction of long-term potentiation in the dentate gyrus of anaesthetized rats
    • Fazeli MS, Breen K, Errington ML, Bliss TVP. Increase in extracellular NCAM and amyloid precursor protein following induction of long-term potentiation in the dentate gyrus of anaesthetized rats. Neurosci Lett. 169:1994;77-80.
    • (1994) Neurosci Lett , vol.169 , pp. 77-80
    • Fazeli, M.S.1    Breen, K.2    Errington, M.L.3    Bliss, T.V.P.4
  • 134
    • 0029556177 scopus 로고
    • Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning
    • Tissue plasminogen activator was significantly induced in the Purkinje neurons of mice performing cerebellar motor tasks compared to control mice. of special interest
    • Seeds NW, Williams BL, Bickford PC. Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning. Science. 270:1995;1992-1994 Tissue plasminogen activator was significantly induced in the Purkinje neurons of mice performing cerebellar motor tasks compared to control mice. of special interest.
    • (1995) Science , vol.270 , pp. 1992-1994
    • Seeds, N.W.1    Williams, B.L.2    Bickford, P.C.3
  • 135
    • 9444240943 scopus 로고    scopus 로고
    • Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways
    • Huang YY, Bach ME, Lipp HP, Zhuo M, Wolfer DP, Hawkins RD, Schoonjans L, Kandel ER, Godfraind JM, Mulligan R, et al. Mice lacking the gene encoding tissue-type plasminogen activator show a selective interference with late-phase long-term potentiation in both Schaffer collateral and mossy fiber pathways. Proc Natl Acad Sci USA. 93:1996;8699-8704.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8699-8704
    • Huang, Y.Y.1    Bach, M.E.2    Lipp, H.P.3    Zhuo, M.4    Wolfer, D.P.5    Hawkins, R.D.6    Schoonjans, L.7    Kandel, E.R.8    Godfraind, J.M.9    Mulligan, R.10
  • 136
    • 0028971072 scopus 로고
    • Induction of beta-A activin expression by synaptic activity and during neocortical development
    • Andreasson K, Worley PF. Induction of beta-A activin expression by synaptic activity and during neocortical development. Neuroscience. 69:1995;781-796.
    • (1995) Neuroscience , vol.69 , pp. 781-796
    • Andreasson, K.1    Worley, P.F.2
  • 137
    • 0030007474 scopus 로고    scopus 로고
    • Narp, a novel member of the pentraxin family, promotes neurite outgrowth and is dynamically regulated by neuronal activity
    • Tsui CC, Copeland NG, Gilbert DJ, Jenkins NA, Barnes C, Worley PF. Narp, a novel member of the pentraxin family, promotes neurite outgrowth and is dynamically regulated by neuronal activity. J Neurosci. 16:1996;2463-2478.
    • (1996) J Neurosci , vol.16 , pp. 2463-2478
    • Tsui, C.C.1    Copeland, N.G.2    Gilbert, D.J.3    Jenkins, N.A.4    Barnes, C.5    Worley, P.F.6
  • 138
    • 0028853459 scopus 로고
    • Arc, a growth factor and activity-regulated gene, encodes a novel cytoskeleton-associated protein that is enriched in neuronal dendrites
    • Following stimulation, both Arc mRNA and protein were induced and enriched in the dendrites. Association of Arc with cytoskeletal elements was suggested both in vivo and in vitro, suggesting a role for Arc in activity-dependent plasticity of dendritic structures. of special interest
    • Lyford GL, Yamagata K, Kaufmann WE, Barnes CA, Sanders LK, Copeland NG, Gilbert DJ, Jenkins NA, Lanahan AA, Worley PF. Arc, a growth factor and activity-regulated gene, encodes a novel cytoskeleton-associated protein that is enriched in neuronal dendrites. Neuron. 14:1995;433-445 Following stimulation, both Arc mRNA and protein were induced and enriched in the dendrites. Association of Arc with cytoskeletal elements was suggested both in vivo and in vitro, suggesting a role for Arc in activity-dependent plasticity of dendritic structures. of special interest.
    • (1995) Neuron , vol.14 , pp. 433-445
    • Lyford, G.L.1    Yamagata, K.2    Kaufmann, W.E.3    Barnes, C.A.4    Sanders, L.K.5    Copeland, N.G.6    Gilbert, D.J.7    Jenkins, N.A.8    Lanahan, A.A.9    Worley, P.F.10
  • 139
    • 0029995029 scopus 로고    scopus 로고
    • COX-2, a synaptically induced enzyme, is expressed by excitatory neurons at postsynaptic sites in rat cerebral cortex
    • Kaufmann WE, Worley PF, Pegg J, Bremer M, Isakson P. COX-2, a synaptically induced enzyme, is expressed by excitatory neurons at postsynaptic sites in rat cerebral cortex. Proc Natl Acad Sci USA. 93:1996;2317-2321.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2317-2321
    • Kaufmann, W.E.1    Worley, P.F.2    Pegg, J.3    Bremer, M.4    Isakson, P.5


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