Postsynaptic translation affects the efficacy and morphology of neuromuscular junctions.
Long-term synaptic plasticity may be associated with structural rearrangements within the neuronal circuitry. Although the molecular mechanisms governing such activity-controlled morphological alterations are mostly elusive, polysomal accumulations at the base of developing dendritic spines and the activity-induced synthesis of synaptic components suggest that localized translation is involved during synaptic plasticity. Here we show that large aggregates of translational components as well as messenger RNA of the postsynaptic glutamate receptor subunit DGluR-IIA are localized within subsynaptic compartments of larval neuromuscular junctions of Drosophila melanogaster. Genetic models of junctional plasticity and genetic manipulations using the translation initiation factors eIF4E and poly(A)-binding protein showed an increased occurrence of subsynaptic translation aggregates. This was associated with a significant increase in the postsynaptic DGluR-IIA protein levels and a reduction in the junctional expression of the cell-adhesion molecule Fasciclin II. In addition, the efficacy of junctional neurotransmission and the size of larval neuromuscular junctions were significantly increased. Our results therefore provide evidence for a postsynaptic translational control of long-term junctional plasticity.
Sigrist
S J
SJ
Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Tübingen, Germany.
Thiel
P R
PR
Reiff
D F
DF
Lachance
P E
PE
Lasko
P
P
Schuster
C M
CM
D000818:Animals; D004331:Drosophila melanogaster / Q000196:embryology / Q000235:genetics / Q000502:physiology; D039561:Eukaryotic Initiation Factor-4E; D005786:Gene Expression Regulation; D007814:Larva; D017774:Long-Term Potentiation / Q000235:genetics / Q000502:physiology; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000235:genetics; D009469:Neuromuscular Junction / Q000196:embryology / Q000502:physiology*; D010448:Peptide Initiation Factors / Q000096:biosynthesis / Q000502:physiology; D039102:Poly(A)-Binding Proteins; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000096:biosynthesis; D018091:Receptors, AMPA / Q000235:genetics / Q000378:metabolism; D013569:Synapses / Q000502:physiology*
D039561:Eukaryotic Initiation Factor-4E; D009419:Nerve Tissue Proteins; D010448:Peptide Initiation Factors; D039102:Poly(A)-Binding Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D018091:Receptors, AMPA; C104722:glutamate receptor ionotropic, AMPA 2