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Mol. Cells 2011; 31(2): 175-180

Published online December 30, 2011

https://doi.org/10.1007/s10059-011-0025-7

© The Korean Society for Molecular and Cellular Biology

State-Dependent Disruption of Short-Term Facilitation Due to Overexpression of the apPDE4 Supershort Form in Aplysia

Deok-Jin Jang1,4,5, Jin-A Lee2,5, Yeon-Su Chae1, and Bong-Kiun Kaang1,3,*

1National Creative Research Initiative Center for Memory, Departments of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 2Department of Biotechnology, College of Life Science and Nano Technology, Hannam University, Daejeon 305-811, Korea, 3Brain and Cognitive Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 4Present address: Department of Applied Biology, College of Ecology and Environment, Kyungpook National University, Sangju 742-711, Korea, 5These authors contributed equally to this work.

Correspondence to : *Correspondence: kaang@snu.ac.kr

Received: October 12, 2010; Revised: November 27, 2010; Accepted: December 7, 2010

Abstract

Phosphodiesterases (PDEs) play important roles in synaptic plasticity by regulating cAMP signaling in various organisms. The supershort, short, and long forms of Aplysia PDE4 (apPDE4) have been cloned, and the long form has been shown to play a crucial role in 5- hydroxytryptamine (5-HT)-induced synaptic plasticity in Aplysia. To address the role of the supershort form in 5-HT-induced synaptic plasticity in Aplysia, we overexpressed the apPDE4 supershort form in Aplysia sensory neurons. Consequently, 5-HT-induced hyperexcitability and short-term facilitation in nondepressed synapses were blocked. However, the su-pershort form did not inhibit 5-HT-induced short-term facilitation in highly depressed synapses. These results show that the supershort form plays an important role in 5-HT-induced synaptic plasticity and disrupts it mainly by impairing cAMP signaling in Aplysia.

Keywords Aplysia, depressed synapse, PDE4, supershort form, synaptic facilitation

Article

Research Article

Mol. Cells 2011; 31(2): 175-180

Published online February 28, 2011 https://doi.org/10.1007/s10059-011-0025-7

Copyright © The Korean Society for Molecular and Cellular Biology.

State-Dependent Disruption of Short-Term Facilitation Due to Overexpression of the apPDE4 Supershort Form in Aplysia

Deok-Jin Jang1,4,5, Jin-A Lee2,5, Yeon-Su Chae1, and Bong-Kiun Kaang1,3,*

1National Creative Research Initiative Center for Memory, Departments of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 2Department of Biotechnology, College of Life Science and Nano Technology, Hannam University, Daejeon 305-811, Korea, 3Brain and Cognitive Sciences, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea, 4Present address: Department of Applied Biology, College of Ecology and Environment, Kyungpook National University, Sangju 742-711, Korea, 5These authors contributed equally to this work.

Correspondence to:*Correspondence: kaang@snu.ac.kr

Received: October 12, 2010; Revised: November 27, 2010; Accepted: December 7, 2010

Abstract

Phosphodiesterases (PDEs) play important roles in synaptic plasticity by regulating cAMP signaling in various organisms. The supershort, short, and long forms of Aplysia PDE4 (apPDE4) have been cloned, and the long form has been shown to play a crucial role in 5- hydroxytryptamine (5-HT)-induced synaptic plasticity in Aplysia. To address the role of the supershort form in 5-HT-induced synaptic plasticity in Aplysia, we overexpressed the apPDE4 supershort form in Aplysia sensory neurons. Consequently, 5-HT-induced hyperexcitability and short-term facilitation in nondepressed synapses were blocked. However, the su-pershort form did not inhibit 5-HT-induced short-term facilitation in highly depressed synapses. These results show that the supershort form plays an important role in 5-HT-induced synaptic plasticity and disrupts it mainly by impairing cAMP signaling in Aplysia.

Keywords: Aplysia, depressed synapse, PDE4, supershort form, synaptic facilitation

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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