mRNA 3′-UTR shortening is a molecular signature of mTORC1 activation

Jae-Woong Chang, Wei Zhang, Hsin-Sung Yeh, Ebbing P. de Jong, Semo Jun, Kwan-Hyun Kim, Sun S. Bae, Kenneth Beckman, Tae Hyun Hwang, Kye-Seong Kim, Do-Hyung Kim, Timothy J. Griffin, Rui Kuang and Jeongsik Yong ()
Additional contact information
Jae-Woong Chang: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Wei Zhang: University of Minnesota
Hsin-Sung Yeh: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Ebbing P. de Jong: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Semo Jun: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Kwan-Hyun Kim: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Sun S. Bae: Pusan National University School of Medicine
Kenneth Beckman: Biomedical Genomics Center, University of Minnesota
Tae Hyun Hwang: Quantitative Biomedical Research Center, University of Texas Southwestern Medical Center
Kye-Seong Kim: Graduate School of Biomedical Science and Engineering, Hanyang University
Do-Hyung Kim: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Timothy J. Griffin: Molecular Biology and Biophysics, University of Minnesota Twin Cities
Rui Kuang: University of Minnesota
Jeongsik Yong: Molecular Biology and Biophysics, University of Minnesota Twin Cities

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract Mammalian target of rapamycin (mTOR) enhances translation from a subset of messenger RNAs containing distinct 5′-untranslated region (UTR) sequence features. Here we identify 3′-UTR shortening of mRNAs as an additional molecular signature of mTOR activation and show that 3′-UTR shortening enhances the translation of specific mRNAs. Using genetic or chemical modulations of mTOR activity in cells or mouse tissues, we show that cellular mTOR activity is crucial for 3′-UTR shortening. Although long 3′-UTR-containing transcripts minimally contribute to translation, 3-′UTR-shortened transcripts efficiently form polysomes in the mTOR-activated cells, leading to increased protein production. Strikingly, selected E2 and E3 components of ubiquitin ligase complexes are enriched by this mechanism, resulting in elevated levels of protein ubiquitination on mTOR activation. Together, these findings identify a previously uncharacterized role for mTOR in the selective regulation of protein synthesis by modulating 3′-UTR length of mRNAs.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms8218 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8218

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8218

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().