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Intracellular Membrane Association of the Aplysia cAMP Phosphodiesterase Long and Short Forms via Different Targeting Mechanisms

Title
Intracellular Membrane Association of the Aplysia cAMP Phosphodiesterase Long and Short Forms via Different Targeting Mechanisms
Authors
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
2014-09-12
Citation
Journal of Biological Chemistry, 289(37), 25797-25811
Type
Article
Article Type
Article
Keywords
3&apos,5&apos-Cyclic-Amp PhosphodiesterasesAmino AcidAmino Acid SequenceAmino AcidsAmino Terminal SequenceAnimalAnimalsAplysiaAssociation ReactionsCell CompartmentalizationCell MembraneCell MembranesCellular DistributionControlled StudyCyclic AMPCyclic AMP PhosphodiesteraseCyclic Nucleotide Phosphodiesterases, Type 4Drug EffectsElectrostaticsEnzyme InhibitionEnzymologyEstersFacilitationGeneticsHydrophobic InteractionsHydrophobicityImmunoprecipitationIntracellular MembraneIntracellular MembranesIntracellular SignalingIsoproteinLipidMembranesMetabolismMolecular MechanicsMolecular MechanismNegatively ChargedNon-HumanOligomerizationPhosphatidylinositolPhosphodiesterasePhosphodiesterase IVPolyphosphoinositideProtein IsoformsProtein MultimerizationSerotoninSignal TransductionStatic ElectricitySubcellular OrganellesSubcellular TargetingSynapseSynapses
ISSN
0021-9258
Abstract
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.
URI
http://hdl.handle.net/20.500.11750/1676
DOI
10.1074/jbc.M114.572222
Publisher
American Society for Biochemistry and Molecular Biology Inc.
Related Researcher
  • Author Suh, Byung Chang Current Lab
  • Research Interests Molecular mechanisms of epilepsy and sensory pain transmission; Signaling mechanism of ion channel regulation and membrane excitability; 분자전기생리; 간질 및 통증의 분자적 기전 연구
Files:
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Collection:
Brain and Cognitive SciencesCurrent Lab1. Journal Articles


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