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Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules

Overview of attention for article published in BMC Molecular and Cell Biology, August 2016
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  • Good Attention Score compared to outputs of the same age (65th percentile)
  • Good Attention Score compared to outputs of the same age and source (66th percentile)

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2 X users
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1 Wikipedia page

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38 Dimensions

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112 Mendeley
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Title
Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules
Published in
BMC Molecular and Cell Biology, August 2016
DOI 10.1186/s12867-016-0072-x
Pubmed ID
Authors

Klara Frydryskova, Tomas Masek, Katerina Borcin, Silvia Mrvova, Veronica Venturi, Martin Pospisek

Abstract

Eukaryotic translation initiation factor 4E (eIF4E) plays a pivotal role in the control of cap-dependent translation initiation, modulates the fate of specific mRNAs, occurs in processing bodies (PBs) and is required for formation of stress granules (SGs). In this study, we focused on the subcellular localization of a representative compendium of eIF4E protein isoforms, particularly on the less studied members of the human eIF4E protein family, eIF4E2 and eIF4E3. We showed that unlike eIF4E1, its less studied isoform eIF4E3_A, encoded by human chromosome 3, localized to stress granules but not PBs upon both heat shock and arsenite stress. Furthermore, we found that eIF4E3_A interacts with human translation initiation factors eIF4G1, eIF4G3 and PABP1 in vivo and sediments into the same fractions as canonical eIF4E1 during polysome analysis in sucrose gradients. Contrary to this finding, the truncated human eIF4E3 isoform, eIF4E3_B, showed no localization to SGs and no binding to eIF4G. We also highlighted that eIF4E2 may exhibit distinct functions under different stresses as it readily localizes to P-bodies during arsenite and heat stresses, whereas it is redirected to stress granules only upon heat shock. We extended our study to a number of protein variants, arising from alternative mRNA splicing, of each of the three eIF4E isoforms. Our results surprisingly uncovered differences in the ability of eIF4E1_1 and eIF4E1_3 to form stress granules in response to cellular stresses. Our comparison of all three human eIF4E isoforms and their protein variants enriches the intriguing spectrum of roles attributed to the eukaryotic initiation translation factors of the 4E family, which exhibit a distinctive localization within different RNA granules under different stresses. The localization of eIF4E3_A to stress granules, but not to processing bodies, along with its binding to eIF4G and PABP1 suggests a role of human eIF4E3_A in translation initiation rather than its involvement in a translational repression and mRNA decay and turnover. The localization of eIF4E2 to stress granules under heat shock but not arsenite stress indicates its distinct function in cellular response to these stresses and points to the variable protein content of SGs as a consequence of different stress insults.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 112 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Canada 1 <1%
Unknown 111 99%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 25 22%
Researcher 20 18%
Student > Master 14 13%
Student > Bachelor 14 13%
Student > Doctoral Student 8 7%
Other 12 11%
Unknown 19 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 42 38%
Agricultural and Biological Sciences 21 19%
Neuroscience 8 7%
Medicine and Dentistry 5 4%
Immunology and Microbiology 3 3%
Other 10 9%
Unknown 23 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 4. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 September 2017.
All research outputs
#7,959,659
of 25,373,627 outputs
Outputs from BMC Molecular and Cell Biology
#277
of 1,233 outputs
Outputs of similar age
#115,445
of 348,145 outputs
Outputs of similar age from BMC Molecular and Cell Biology
#5
of 15 outputs
Altmetric has tracked 25,373,627 research outputs across all sources so far. This one has received more attention than most of these and is in the 67th percentile.
So far Altmetric has tracked 1,233 research outputs from this source. They receive a mean Attention Score of 4.0. This one has done well, scoring higher than 75% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 348,145 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 65% of its contemporaries.
We're also able to compare this research output to 15 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 66% of its contemporaries.