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Whereas binding of pp90rsk inhibits CREB-mediated gene induction, it is required for Ras-mediated gene expression. of special interest
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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.
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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.
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Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha
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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.
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Livingston, D.M.7
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Control of cAMP-regulated enhancers by the viral transactivator Tax through CREB and the co-activator CBP
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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
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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.
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Kwok, R.P.1
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Bannister, A.J.1
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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
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105
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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.
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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.
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Enslen, H.1
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114
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116
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The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
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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.
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119
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Regulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elements
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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
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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.
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Robertson, L.M.1
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120
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15844416253
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Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity
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See annotation [122]. of outstanding interest
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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.
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Loh, C.1
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Luo, C.5
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Rao, A.7
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121
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Shibasaki, F.1
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122
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0029851762
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2+ signals and immunosuppression
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2+ influx is terminated, NFAT is rapidly exported from the nucleus, presumably after rephosphorylation. of outstanding interest
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2+ influx is terminated, NFAT is rapidly exported from the nucleus, presumably after rephosphorylation. of outstanding interest.
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Nature
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Timmerman, L.A.1
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125
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15144343374
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Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: Role in EGF receptor-mediated tyrosine phosphorylation
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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
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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.
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Bae, Y.S.1
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126
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Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of STAT1
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Shuai, K.1
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127
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The rapid inactivation of nuclear tyrosine phosphorylated STAT1 depends upon a protein tyrosine phosphatase
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Haspel, R.L.1
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Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learning
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134
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Tissue plasminogen activator induction in Purkinje neurons after cerebellar motor learning
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Seeds, N.W.1
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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
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Narp, a novel member of the pentraxin family, promotes neurite outgrowth and is dynamically regulated by neuronal activity
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138
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0028853459
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Arc, a growth factor and activity-regulated gene, encodes a novel cytoskeleton-associated protein that is enriched in neuronal dendrites
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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
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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.
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Gilbert, D.J.7
Jenkins, N.A.8
Lanahan, A.A.9
Worley, P.F.10
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COX-2, a synaptically induced enzyme, is expressed by excitatory neurons at postsynaptic sites in rat cerebral cortex
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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.
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Kaufmann, W.E.1
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Pegg, J.3
Bremer, M.4
Isakson, P.5
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