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Intracellular Membrane Association of the Aplysia cAMP Phosphodiesterase Long and Short Forms via Different Targeting Mechanisms
- Intracellular Membrane Association of the Aplysia cAMP Phosphodiesterase Long and Short Forms via Different Targeting Mechanisms
- Kim, KH[Kim, Kun-Hyung]; Jun, YW[Jun, Yong-Woo]; Park, Y[Park, Yongsoo]; Lee, JA[Lee, Jin-A]; Suh, BC[Suh, Byung-Chang]; Lim, CS[Lim, Chae-Seok]; Lee, YS[Lee, Yong-Seok]; Kaang, BK[Kaang, Bong-Kiun]; Jang, DJ[Jang, Deok-Jin]
- DGIST Authors
- Suh, BC[Suh, Byung-Chang]
- Issue Date
- Journal of Biological Chemistry, 289(37), 25797-25811
- Article Type
- 3' ,5' -Cyclic-Amp Phosphodiesterases; Amino Acid; Amino Acid Sequence; Amino Acids; Amino Terminal Sequence; Animal; Animals; Aplysia; Association Reactions; Cell Compartmentalization; Cell Membrane; Cell Membranes; Cellular Distribution; Controlled Study; Cyclic AMP; Cyclic AMP Phosphodiesterase; Cyclic Nucleotide Phosphodiesterases, Type 4; Drug Effects; Electrostatics; Enzyme Inhibition; Enzymology; Esters; Facilitation; Genetics; Hydrophobic Interactions; Hydrophobicity; Immunoprecipitation; Intracellular Membrane; Intracellular Membranes; Intracellular Signaling; Isoprotein; Lipid; Membranes; Metabolism; Molecular Mechanics; Molecular Mechanism; Negatively Charged; Non-Human; Oligomerization; Phosphatidylinositol; Phosphodiesterase; Phosphodiesterase IV; Polyphosphoinositide; Protein Isoforms; Protein Multimerization; Serotonin; Signal Transduction; Static Electricity; Subcellular Organelles; Subcellular Targeting; Synapse; Synapses
- Phosphodiesterases (PDEs) play key roles in cAMP compartmentalization, which is required for intracellular signaling processes, through specific subcellular targeting. Previously, we showed that the long and short forms of Aplysia PDE4 (ApPDE4), which are localized to the membranes of distinct subcellular organelles, play key roles in 5-hydroxytryptamineinduced synaptic facilitation in Aplysia sensory and motor synapses. However, the molecular mechanism of the isoform-specific distinct membrane targeting was not clear. In this study, we further investigated the molecular mechanism of the membrane targeting of the ApPDE4 long and short forms. We found that the membrane targeting of the long form was mediated by hydrophobic interactions, mainly via 16 amino acids at the N-terminal region, whereas the short form was targeted solely to the plasma membrane, mainly by nonspecific electrostatic interactions between theirNtermini and the negatively charged lipids such as the phosphatidylinositol polyphosphates PI4P and PI(4,5)P2, which are embedded in the inner leaflet of the plasma membrane. Moreover, oligomerization of the long or short form by interaction of their respective upstream conserved region domains, UCR1 and UCR2, enhanced their plasma membrane targeting. These results suggest that the long and short forms of ApPDE4 are distinctly targeted to intracellular membranes through their direct association with the membranes via hydrophobic and electrostatic interactions, respectively. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
- American Society for Biochemistry and Molecular Biology Inc.
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