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Cited by 117RNA Research and SplicingPI3K/AKT/mTOR signaling in cancerRNA and protein synthesis mechanisms

Degradation of high affinity HuD targets releases Kv1.1 mRNA from miR-129 repression by mTORC1

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Sosanya, Natasha M., Huang, Peggy P.C., Cacheaux, Luisa P., Chen, Chun Jung, Nguyen, Kathleen, Perrone-Bizzozero, Nora I., Raab-Graham, Kimberly F.·2013·Journal of Cell Biology
DOI 10.1083/jcb.201212089PMC PMC3704988
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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.

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Cited by

Sorted by citations

Authors
Sosanya, N. M., Huang, P. P. C., Cacheaux, L. P., Chen, C. J., Nguyen, K., Perrone-Bizzozero, N. I., & Raab-Graham, K. F.
Affiliations
  • The University of Texas at Austin (US)
  • Texas A&M Health Science Center (US)
  • Department of Neurosciences, University of New Mexico Health Sciences Center, Albuquerque, NM 87131 4
  • Center for Learning and Memory, Section of Neurobiology 1 ; and 2
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2013-07-08
Volume
202
Issue
1
Pages
53-69
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201212089
PMC
PMC3704988
OpenAlex
W2102885253
Cited by
117
References
4
Citations by year
2026: 2 · 2025: 6 · 2024: 4 · 2023: 7 · 2022: 5 · 2021: 6 · 2020: 16 · 2019: 6 · 2018: 12 · 2017: 12 · 2016: 10 · 2015: 12 · 2014: 15 · 2013: 4
FWCI
6.13
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • OakTrust (Texas A&M University Libraries) (submittedVersion)
Funders
  • National Institute on Drug Abuse (R01DA034097)
  • National Institute of Neurological Disorders and Stroke (R01NS030255, 5R01-NS30255)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
Kv1.1, mTORC1, miR-129, HUD, mRNA degradation, mRNA stability, translational regulation, microRNA repression, voltage-gated potassium channels, dendritic ion channels, neuronal excitability, RNA-binding proteins, dendritic mRNA
MeSH terms
ELAV-Like Protein 4, Mechanistic Target of Rapamycin Complex 1, Animals, Binding Sites, Enzyme Activation, Humans, Neuronal Plasticity, Neurons, Proteins, Repressor Proteins, RNA Processing, Post-Transcriptional, RNA, Messenger, Transfection, Protein Biosynthesis, Signal Transduction, RNA Stability, MicroRNAs, Multiprotein Complexes, Rats, Kv1.1 Potassium Channel, ELAV Proteins, HEK293 Cells, TOR Serine-Threonine Kinases, Proteolysis

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