ArticleProceedings of the National Academy of Sciences of the United States of America1990
Protein synthesis during acquisition of long-term facilitation is needed for the persistent loss of regulatory subunits of the Aplysia cAMP-dependent protein kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 78 citations in OpenAlex.
- Decoding the complex journeys of RNAs along neurons.Nucleic acids research · 2025Article
- Ubiquitination in postsynaptic function and plasticity.Annual review of cell and developmental biology · 2010Review
- Serotonin induces selective cleavage of the PKA RI subunit but not RII subunit in Aplysia neurons.Biochemical and biophysical research communications · 2007Article
- Protein synthesis required for long-term memory is induced by PKC activation on days before associative learning.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Substance P modulates NMDA responses and causes long-term protein synthesis-dependent modulation of the lamprey locomotor network.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Rheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals.Molecular and cellular biology · 1997Article
- Toward a molecular definition of long-term memory storage.Proceedings of the National Academy of Sciences of the United States of America · 1996Review
- Ethanol causes translocation of cAMP-dependent protein kinase catalytic subunit to the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Induction of long-term facilitation in Aplysia sensory neurons by local application of serotonin to remote synapses.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: a molecular mechanism underlying long-term synaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Spinal-Cord plasticity: independent and interactive effects of neuromodulator and activity-dependent plasticity.Molecular neurobiologyReview
- Ubiquitin-mediated proteolysis in learning and memory.Molecular neurobiologyReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Depending on the number or the length of exposure, application of serotonin can produce either short-term or long-term presynaptic facilitation of Aplysia sensory-to-motor synapses. The cAMP-dependent protein kinase, a heterodimer of two regulatory and two catalytic subunits, has been shown to become stably activated only during long-term facilitation. Both acquisition of long-term facilitation and persistent activation of the kinase is blocked by anisomycin, an effective, reversible, and specific inhibitor of protein synthesis in Aplysia. We report here that 2-hr exposure of pleural sensory cells to serotonin lowers the concentration of regulatory subunits but does not change the concentration of catalytic subunits, as assayed 24 hr later; 5-min exposure to serotonin has no effect on either type of subunit. Increasing intracellular cAMP with a permeable analog of cAMP together with the phosphodiesterase inhibitor isobutyl methylxanthine also decreased regulatory subunits, suggesting that cAMP is the second messenger mediating serotonin action. Anisomycin blocked the loss of regulatory subunits only when applied with serotonin; application after the 2-hr treatment with serotonin had no effect. In the Aplysia accessory radula contractor muscle, prolonged exposure to serotonin or to the peptide transmitter small cardioactive peptide B, both of which produce large increases in intracellular cAMP, does not decrease regulatory subunits. This mechanism of regulating the cAMP-dependent protein kinase therefore may be specific to the nervous system. We conclude that during long-term facilitation, new protein is synthesized in response to the facilitatory stimulus, which changes the ratio of subunits of the cAMP-dependent protein kinase. This alteration in ratio could persistently activate the kinase and produce the persistent phosphorylation seen in long-term facilitated sensory cells.
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