S6K1 Phosphorylates and Regulates Fragile X Mental Retardation Protein (FMRP) with the Neuronal Protein Synthesis-dependent Mammalian Target of Rapamycin (mTOR) Signaling Cascade *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 283, Issue: 27, Page: 18478-18482
2008
- 179Citations
- 74Usage
- 192Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations179
- Citation Indexes179
- 179
- CrossRef153
- Usage74
- Abstract Views74
- Captures192
- Readers192
- 189
Article Description
Fragile X syndrome is a common form of cognitive deficit caused by the functional absence of fragile X mental retardation protein (FMRP), a dendritic RNA-binding protein that represses translation of specific messages. Although FMRP is phosphorylated in a group I metabotropic glutamate receptor (mGluR) activity-dependent manner following brief protein phosphatase 2A (PP2A)-mediated dephosphorylation, the kinase regulating FMRP function in neuronal protein synthesis is unclear. Here we identify ribosomal protein S6 kinase (S6K1) as a major FMRP kinase in the mouse hippocampus, finding that activity-dependent phosphorylation of FMRP by S6K1 requires signaling inputs from mammalian target of rapamycin (mTOR), ERK1/2, and PP2A. Further, the loss of hippocampal S6K1 and the subsequent absence of phospho-FMRP mimic FMRP loss in the increased expression of SAPAP3, a synapse-associated FMRP target mRNA. Together these data reveal a S6K1-PP2A signaling module regulating FMRP function and place FMRP phosphorylation in the mGluR-triggered signaling cascade required for protein-synthesis-dependent synaptic plasticity.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002192582081446X; http://dx.doi.org/10.1074/jbc.c800055200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=49649106751&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18474609; http://www.jbc.org/lookup/doi/10.1074/jbc.C800055200; https://syndication.highwire.org/content/doi/10.1074/jbc.C800055200; https://linkinghub.elsevier.com/retrieve/pii/S002192582081446X; https://escholarship.umassmed.edu/gsbs_sp/1501; https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2500&context=gsbs_sp; https://dx.doi.org/10.1074/jbc.c800055200; http://www.jbc.org/content/283/27/18478; http://www.jbc.org/article/S002192582081446X/abstract; http://www.jbc.org/article/S002192582081446X/fulltext; http://www.jbc.org/article/S002192582081446X/pdf; https://www.jbc.org/article/S0021-9258(20)81446-X/abstract; http://www.jbc.org/cgi/doi/10.1074/jbc.C800055200; http://www.jbc.org/content/283/27/18478.abstract; http://www.jbc.org/content/283/27/18478.full; http://www.jbc.org/content/283/27/18478.full.pdf
American Society for Biochemistry & Molecular Biology (ASBMB)
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