Details

Autor(en) / Beteiligte

• Huang, Yi-Shuian
• Jung, Mi-Young
• Sarkissian, Madathia
• Richter, Joel D.

Titel

N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses

Ist Teil von

• The EMBO journal, 2002-05, Vol.21 (9), p.2139-2148

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2002

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.