An Aplysia type 4 phosphodiesterase homolog localizes at the presynaptic terminals of Aplysia neuron and regulates synaptic facilitation

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The cAMP-dependent signaling pathway is critically involved in memory-related synaptic plasticity. cAMP-specific type 4 phosphodiesterases (PDE4) play a role in this process by regulating the cAMP concentration. However, it is unclear how PDE4 is involved in regulating synaptic plasticity. To address this issue in Aplysia sensory-to-motor synapses, we identified a long isoform of the PDE4 homolog in Aplysia kurodai (apPDE), with genetic and biochemical properties similar to those of mammalian PDE4s. Furthermore, apPDE is localized to the membrane and presynaptic region. Both apPDE overexpression and knock-down impaired short- and long-term facilitation, indicating that an appropriate expression level of apPDE in synaptic regions is required for normal synaptic facilitation. By using fluorescence resonance energy transfer-based measurement of in vivo protein kinase A (PKA) activation, we found that the PKA activation by 5-hydroxytryptamine (5-HT) was impaired in both apPDE-overexpressed and knock-down synapses. Analogous to the inhibition of apPDE by RNA interference, chronic rolipram treatment before 5-HT stimulation also impaired the PKA activation by 5-HT, suggesting that regulation of the synaptic cAMP level by PDE4 is critical for normal synaptic facilitation. Together, we suggest that PDE4s localized in the synapses play a critical role in regulating the optimum cAMP level required for normal synaptic plasticity.
Publisher
SOC NEUROSCIENCE
Issue Date
2005-09
Language
English
Article Type
Article
Keywords

LONG-TERM FACILITATION; CYCLIC-NUCLEOTIDE PHOSPHODIESTERASES; DEPENDENT PROTEIN-KINASE; CAMP-SPECIFIC PHOSPHODIESTERASE; SENSORY NEURONS; ADENYLYL-CYCLASE; MEMBRANE ASSOCIATION; MOLECULAR-CLONING; RNA INTERFERENCE; SPLICE VARIANTS

Citation

JOURNAL OF NEUROSCIENCE, v.25, no.39, pp.9037 - 9045

ISSN
0270-6474
DOI
10.1523/JNEUROSCI.1989-05.2005
URI
http://hdl.handle.net/10203/255879
Appears in Collection
BS-Journal Papers(저널논문)
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