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http://dx.doi.org/10.5806/AST.2016.29.1.10

Analysis of molecular mechanism of cellular localization of various N-terminal mutants of Aplysia PDE4 in HEK293T cells  

Um, Su-Min (Department of Applied Biology, College of Ecology and Environment, Kyungpook National University)
Jun, Yong-Woo (Ecological Science, College of Ecology and Environment, Kyungpook National University)
Kim, Kun-Hyung (Ecological Science, College of Ecology and Environment, Kyungpook National University)
Lee, Jin-A (Department of Biological Science and Biotechnology, College of Life Science and Nano Technology, Hannam University)
Jang, Deok-Jin (Department of Applied Biology, College of Ecology and Environment, Kyungpook National University)
Publication Information
Analytical Science and Technology / v.29, no.1, 2016 , pp. 10-18 More about this Journal
Abstract
Phosphodiesterase (PDE) plays an important role in cAMP-mediated signaling within cells. We previously showed that the long-form of Aplysia PDE4 (ApPDE4) was localized in the plasma membrane and the presynaptic terminal in Aplysia sensory neurons, and the 16 N-terminal amino acid was sufficient for this targeting process. In this study, we characterized the cellular localization of various ApPDE4 mutants. We first identified the roles of each amino acid within the group of 16 N-terminal amino acids of long-form ApPDE4. As a result, we were able to identify various mutants that were localized to both the plasma membrane and the Golgi complex, Golgi only, or both the endoplasmic reticulum (ER) and the Golgi complex. To examine the role of palmitoylation on the cellular localization of ApPDE4 mutants, 2-bromo palmitate (2-BR) was used as a treatment. As a result, in the presence of 2-BR, the plasma membrane targeting of many mutants was impaired, indicating that palmitoylation was involved in the plasma membrane targeting of the mutants. We also found that PI4P play crucial roles in the Golgi targeting of (N16,C3S/VV/G)-mRFP, L(N16,C3S/LFS/R)-mRFP, and L(N16,EPL/R)-mRFP.
Keywords
Aplysia; phosphodiesteras 4; plasma membrane; Golgi complex; PI4P; palmitoylation;
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