Evidence map›Paper›PMID 24091728›Full record

ArticleCell cycle (Georgetown, Tex.)2013

Phosphorylation of eIF4GII and 4E-BP1 in response to nocodazole treatment: a reappraisal of translation initiation during mitosis.

Mark J Coldwell, Joanne L Cowan, Markete Vlasak, Abbie Mead, Mark Willett, Lisa S Perry, Simon J Morley

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 55 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Mark J ColdwellCentre for Biological Sciences; University of Southampton; Southampton, UK.
Joanne L Cowan
Markete Vlasak
Abbie Mead
Mark Willett
Lisa S Perry
Simon J Morley
University of Southampton · GBUniversity of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D007593/1Biotechnology and Biological Sciences Research Council BB/H006834/1
6 · The paper itself

Abstract

Translation mechanisms at different stages of the cell cycle have been studied for many years, resulting in the dogma that translation rates are slowed during mitosis, with cap-independent translation mechanisms favored to give expression of key regulatory proteins. However, such cell culture studies involve synchronization using harsh methods, which may in themselves stress cells and affect protein synthesis rates. One such commonly used chemical is the microtubule de-polymerization agent, nocodazole, which arrests cells in mitosis and has been used to demonstrate that translation rates are strongly reduced (down to 30% of that of asynchronous cells). Using synchronized HeLa cells released from a double thymidine block (G 1/S boundary) or the Cdk1 inhibitor, RO3306 (G 2/M boundary), we have systematically re-addressed this dogma. Using FACS analysis and pulse labeling of proteins with labeled methionine, we now show that translation rates do not slow as cells enter mitosis. This study is complemented by studies employing confocal microscopy, which show enrichment of translation initiation factors at the microtubule organizing centers, mitotic spindle, and midbody structure during the final steps of cytokinesis, suggesting that translation is maintained during mitosis. Furthermore, we show that inhibition of translation in response to extended times of exposure to nocodazole reflects increased eIF2α phosphorylation, disaggregation of polysomes, and hyperphosphorylation of selected initiation factors, including novel Cdk1-dependent N-terminal phosphorylation of eIF4GII. Our work suggests that effects on translation in nocodazole-arrested cells might be related to those of the treatment used to synchronize cells rather than cell cycle status.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAntineoplastic AgentsCDC2 Protein KinaseCell Cycle ProteinsCytokinesiseIF-2 KinaseEukaryotic Initiation Factor-4GHeLa CellsHumansMass SpectrometryMitosisMolecular Sequence DataNocodazolePeptidesPhosphoproteinsAdaptor Proteins, Signal TransducingAntineoplastic AgentsCDC2 Protein KinaseCell Cycle ProteinsEIF2AK1 protein, humaneIF-2 KinaseEIF4EBP1 protein, humanEIF4G2 protein, humanEukaryotic Initiation Factor-4GNocodazolePeptidesPhosphoproteinsQuinolinesRO 3306ThiazolesTubulin4E-BP1Cdk1cell cycleeIF4GIIeukaryotic translation initiation factornocodazole

Identifiers

PMID24091728
PMCPMC3903713
OpenAlexW2000473050

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.