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Granules Harboring Translationally Active MRNAs Provide a Platform for P-body Formation Following Stress

Overview
Journal Cell Rep
Publisher Cell Press
Date 2014 Dec 2
PMID 25437551
Citations 33
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Abstract

The localization of mRNA to defined cytoplasmic sites in eukaryotic cells not only allows localized protein production but also determines the fate of mRNAs. For instance, translationally repressed mRNAs localize to P-bodies and stress granules where their decay and storage, respectively, are directed. Here, we find that several mRNAs are localized to granules in unstressed, actively growing cells. These granules play a key role in the stress-dependent formation of P-bodies. Specific glycolytic mRNAs are colocalized in multiple granules per cell, which aggregate during P-body formation. Such aggregation is still observed under conditions or in mutants where P-bodies do not form. In unstressed cells, the mRNA granules appear associated with active translation; this might enable a coregulation of protein expression from the same pathways or complexes. Parallels can be drawn between this coregulation and the advantage of operons in prokaryotic systems.

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References
1.
Ashe M, De Long S, Sachs A . Glucose depletion rapidly inhibits translation initiation in yeast. Mol Biol Cell. 2000; 11(3):833-48. PMC: 14814. DOI: 10.1091/mbc.11.3.833. View

2.
Willett M, Brocard M, Davide A, Morley S . Translation initiation factors and active sites of protein synthesis co-localize at the leading edge of migrating fibroblasts. Biochem J. 2011; 438(1):217-27. DOI: 10.1042/BJ20110435. View

3.
Anand M, Chakraburtty K, Marton M, Hinnebusch A, Kinzy T . Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3. J Biol Chem. 2002; 278(9):6985-91. DOI: 10.1074/jbc.M209224200. View

4.
Reijns M, Alexander R, Spiller M, Beggs J . A role for Q/N-rich aggregation-prone regions in P-body localization. J Cell Sci. 2008; 121(Pt 15):2463-72. PMC: 2680509. DOI: 10.1242/jcs.024976. View

5.
Jackson R, Standart N . How do microRNAs regulate gene expression?. Sci STKE. 2007; 2007(367):re1. DOI: 10.1126/stke.3672007re1. View