Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 6, Pages 732-U106Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1815
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Funding
- National Institute on Aging, US National Institutes of Health
- [DA00266]
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Amyloid precursor protein (APP) regulates neuronal synapse function, and its cleavage product Ab is linked to Alzheimer's disease. Here, we present evidence that the RNA-binding proteins (RBPs) heterogeneous nuclear ribonucleoprotein (hnRNP) C and fragile X mental retardation protein (FMRP) associate with the same APP mRNA coding region element, and they influence APP translation competitively and in opposite directions. Silencing hnRNP C increased FMRP binding to APP mRNA and repressed APP translation, whereas silencing FMRP enhanced hnRNP C binding and promoted translation. Repression of APP translation was linked to colocalization of FMRP and tagged APP RNA within processing bodies; this colocalization was abrogated by hnRNP C overexpression or FMRP silencing. Our findings indicate that FMRP represses translation by recruiting APP mRNA to processing bodies, whereas hnRNP C promotes APP translation by displacing FMRP, thereby relieving the translational block.
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