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- W2102885253 abstract "Little is known about how a neuron undergoes site-specific changes in intrinsic excitability during neuronal activity. We provide evidence for a novel mechanism for mTORC1 kinase–dependent translational regulation of the voltage-gated potassium channel Kv1.1 messenger RNA (mRNA). We identified a microRNA, miR-129, that repressed Kv1.1 mRNA translation when mTORC1 was active. When mTORC1 was inactive, we found that the RNA-binding protein, HuD, bound to Kv1.1 mRNA and promoted its translation. Unexpectedly, inhibition of mTORC1 activity did not alter levels of miR-129 and HuD to favor binding to Kv1.1 mRNA. However, reduced mTORC1 signaling caused the degradation of high affinity HuD target mRNAs, freeing HuD to bind Kv1.1 mRNA. Hence, mTORC1 activity regulation of mRNA stability and high affinity HuD-target mRNA degradation mediates the bidirectional expression of dendritic Kv1.1 ion channels." @default.
- W2102885253 created "2016-06-24" @default.
- W2102885253 creator A5026184632 @default.
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- W2102885253 creator A5032390399 @default.
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- W2102885253 creator A5051237501 @default.
- W2102885253 creator A5054786558 @default.
- W2102885253 creator A5075001427 @default.
- W2102885253 date "2013-07-08" @default.
- W2102885253 modified "2023-10-10" @default.
- W2102885253 title "Degradation of high affinity HuD targets releases Kv1.1 mRNA from miR-129 repression by mTORC1" @default.
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- W2102885253 doi "https://doi.org/10.1083/jcb.201212089" @default.
- W2102885253 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3704988" @default.
- W2102885253 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23836929" @default.
- W2102885253 hasPublicationYear "2013" @default.
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