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| Subject Categories: Signal Transduction | Neuroscience |
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| The EMBO Journal
(2002) 21, 2139–2148, doi: 10.1093/emboj/21.9.2139 |
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N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and  CaMKII mRNA polyadenylation at synapses |
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| Yi-Shuian Huang1, 2, Mi-Young Jung1, 2, Madathia Sarkissian1 and Joel D. Richter1 |
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1 Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA 2 Y.-S.Huang and M.-Y.Jung contributed equally to this work To whom correspondence should be addressed Joel D. Richter, joel.richter@umassmed.edu Received 11 January 2002; Revised 11 March 2002; Accepted 15 March 2002. |
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| Abstract |
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| Activity-dependent local translation of dendritic mRNAs is one process that underlies synaptic plasticity. Here, we demonstrate that several of the factors known to control polyadenylation-induced translation in early vertebrate development [cytoplasmic polyadenylation element-binding protein (CPEB), maskin, poly(A) polymerase, cleavage and polyadenylation specificity factor (CPSF) and Aurora] also reside at synaptic sites of rat hippocampal neurons. The induction of polyadenylation at synapses is mediated by the N-methyl-D-aspartate (NMDA) receptor, which transduces a signal that results in the activation of Aurora kinase. This kinase in turn phosphorylates CPEB, an essential RNA-binding protein, on a critical residue that is necessary for polyadenylation-induced translation. These data demonstrate a remarkable conservation of the regulatory machinery that controls signal-induced mRNA translation, and elucidates an axis connecting the NMDA receptor to localized protein synthesis at synapses. |
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| Keywords: polyadenylation, protein phosphorylation, synapse, translation |
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