The impact of microRNAs on protein output

Daehyun Baek, Judit Villén, Chanseok Shin, Fernando D. Camargo, Steven P. Gygi () and David P. Bartel ()
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Daehyun Baek: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA
Judit Villén: 240 Longwood Avenue, Harvard Medical School, Boston, Massachusetts 02115, USA
Chanseok Shin: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA
Fernando D. Camargo: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA
Steven P. Gygi: 240 Longwood Avenue, Harvard Medical School, Boston, Massachusetts 02115, USA
David P. Bartel: Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA

Nature, 2008, vol. 455, issue 7209, 64-71

Abstract: Abstract MicroRNAs are endogenous ∼23-nucleotide RNAs that can pair to sites in the messenger RNAs of protein-coding genes to downregulate the expression from these messages. MicroRNAs are known to influence the evolution and stability of many mRNAs, but their global impact on protein output had not been examined. Here we use quantitative mass spectrometry to measure the response of thousands of proteins after introducing microRNAs into cultured cells and after deleting mir-223 in mouse neutrophils. The identities of the responsive proteins indicate that targeting is primarily through seed-matched sites located within favourable predicted contexts in 3′ untranslated regions. Hundreds of genes were directly repressed, albeit each to a modest degree, by individual microRNAs. Although some targets were repressed without detectable changes in mRNA levels, those translationally repressed by more than a third also displayed detectable mRNA destabilization, and, for the more highly repressed targets, mRNA destabilization usually comprised the major component of repression. The impact of microRNAs on the proteome indicated that for most interactions microRNAs act as rheostats to make fine-scale adjustments to protein output.

Date: 2008
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DOI: 10.1038/nature07242

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