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Vol. 17, No. 5, pp. 638-653, March 1, 2003
1 Program in Molecular Medicine, University of
Massachusetts Medical School, Worcester, Massachusetts 01605, USA;
2 Departments of Biochemistry and 3 Neuroscience,
University of Connecticut Health Center,
Farmington, Connecticut 06030, USA
In neurons, the proteins derived from mRNAs localized in dendrites
have been implicated in synaptic plasticity. The cytoplasmic polyadenylation element (CPE), a cis element in the 3'-UTRs of specific
dendritic mRNAs, promotes cytoplasmic polyadenylation-induced translation in response to synaptic stimulation. Here, we demonstrate that the CPE and its binding protein CPEB facilitate mRNA transport to
dendrites. In rat hippocampal neurons infected with recombinant viruses, the CPE is sufficient to direct a reporter RNA into dendrites. CPEB-GFP protein forms RNA-containing particles that are transported into dendrites in a microtubule-dependent fashion at an average velocity of 4-8 µm/min. Such particles also contain maskin, a CPEB-associated factor that mediates cap-dependent translational repression of CPE-containing mRNA, and the molecular motors dynein and
kinesin. Overexpression of CPEB in neurons promotes the transport of
CPE-containing endogenous MAP2 mRNA to dendrites, whereas
overexpression of a mutant CPEB that is defective for interaction with
molecular motors inhibits this transport. In neurons derived from CPEB
knockout mice, the dendritic transport of a CPE-containing reporter RNA is reduced. These results suggest a mechanism whereby CPE-containing mRNAs can be transported to dendrites in a translationally dormant form, but activated at synapses in response to NMDA receptor stimulation.
[Keywords: synapse; CPEB; maskin; mRNA transport]
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