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Differential Regulation of Proton-Sensitive Ion Channels by Phospholipids: A Comparative Study between ASICs and TRPV1

Title
Differential Regulation of Proton-Sensitive Ion Channels by Phospholipids: A Comparative Study between ASICs and TRPV1
Authors
Kweon, HJ[Kweon, Hae-Jin]Yu, SY[Yu, Soo-Young]Kim, DI[Kim, Dong-Il]Suh, BC[Suh, Byung-Chang]
DGIST Authors
Kweon, HJ[Kweon, Hae-Jin]; Yu, SY[Yu, Soo-Young]; Kim, DI[Kim, Dong-Il]; Suh, BC[Suh, Byung-Chang]
Issue Date
2015-03-17
Citation
PLoS ONE, 10(3)
Type
Article
Article Type
Article
Keywords
Acid-Sensing Ion ChannelArachidonic AcidBinding AffinityChimeric ProteinComparative StudyControlled StudyEmbryoHumanHuman CellPhosphatidylinositidePhosphatidylinositol 3,4,5 Trisphosphate 3 PhosphatasePhosphatidylinositol 4 PhosphatePhosphatidylinositol 4,5 BisphosphateProtein DegradationProtein DephosphorylationProtein DepletionProtein FunctionProtein Lipid InteractionProtein LocalizationProtein PhosphorylationProtein ProcessingProtein TransportSignal TransductionTransient Receptor Potential Channel1
ISSN
1932-6203
Abstract
Protons are released in pain-generating pathological conditions such as inflammation, ischemic stroke, infection, and cancer. During normal synaptic activities, protons are thought to play a role in neurotransmission processes. Acid-sensing ion channels (ASICs) are typical proton sensors in the central nervous system (CNS) and the peripheral nervous system (PNS). In addition to ASICs, capsaicin- and heat-activated transient receptor potential vanilloid 1 (TRPV1) channels can also mediate proton-mediated pain signaling. In spite of their importance in perception of pH fluctuations, the regulatory mechanisms of these proton-sensitive ion channels still need to be further investigated. Here, we compared regulation of ASICs and TRPV1 by membrane phosphoinositides, which are general cofactors of many receptors and ion channels. We observed that ASICs do not require membrane phosphatidylinositol 4-phosphate (PI(4)P) or phosphatidylinositol 4,5-bisphosphate (PI(4,5) P2) for their function. However, TRPV1 currents were inhibited by simultaneous breakdown of PI (4)P and PI(4,5)P2. By using a novel chimeric protein, CF-PTEN, that can specifically dephosphorylate at the D3 position of phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3), we also observed that neither ASICs nor TRPV1 activities were altered by depletion of PI (3,4,5)P3 in intact cells. Finally, we compared the effects of arachidonic acid (AA) on two proton-sensitive ion channels. We observed that AA potentiates the currents of both ASICs and TRPV1, but that they have different recovery aspects. In conclusion, ASICs and TRPV1 have different sensitivities toward membrane phospholipids, such as PI(4)P, PI(4,5) P2, and AA, although they have common roles as proton sensors. Further investigation about the complementary roles and respective contributions of ASICs and TRPV1 in proton-mediated signaling is necessary. © 2015 Kweon et al.
URI
http://hdl.handle.net/20.500.11750/1575
DOI
10.1371/journal.pone.0122014
Publisher
Public Library of Science
Related Researcher
Files:
There are no files associated with this item.
Collection:
Brain and Cognitive SciencesETC1. Journal Articles
Brain and Cognitive SciencesETC1. Journal Articles


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