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- W2103712423 abstract "Abstract Although neurons are highly polarized, how neuronal polarity is generated remains poorly understood. An evolutionarily conserved inositol-producing enzyme myo-inositol monophosphatase (IMPase) is essential for polarized localization of synaptic molecules in Caenorhabditis elegans and can be inhibited by lithium, a drug for bipolar disorder. The synaptic defect of IMPase mutants causes defects in sensory behaviors including thermotaxis. Here we show that the abnormalities of IMPase mutants can be suppressed by mutations in two enzymes, phospholipase Cβ or synaptojanin, which presumably reduce the level of membrane phosphatidylinositol 4,5-bisphosphate (PIP2). We also found that mutations in phospholipase Cβ conferred resistance to lithium treatment. Our results suggest that reduction of PIP2 on plasma membrane is a major cause of abnormal synaptic polarity in IMPase mutants and provide the first in vivo evidence that lithium impairs neuronal PIP2 synthesis through inhibition of IMPase. We propose that the PIP2 signaling regulated by IMPase plays a novel and fundamental role in the synaptic polarity." @default.
- W2103712423 created "2016-06-24" @default.
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- W2103712423 creator A5047109288 @default.
- W2103712423 creator A5083504396 @default.
- W2103712423 creator A5087542585 @default.
- W2103712423 date "2012-06-01" @default.
- W2103712423 modified "2023-10-12" @default.
- W2103712423 title "Synaptic Polarity Depends on Phosphatidylinositol Signaling Regulated by<i>myo</i>-Inositol Monophosphatase in<i>Caenorhabditis elegans</i>" @default.
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- W2103712423 doi "https://doi.org/10.1534/genetics.111.137844" @default.
- W2103712423 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3374314" @default.
- W2103712423 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22446320" @default.
- W2103712423 hasPublicationYear "2012" @default.
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