Evidence map›Paper›PMID 30540951›Full record

ArticleCell reports2018

CDK Phosphorylation of Translation Initiation Factors Couples Protein Translation with Cell-Cycle Transition.

Tai An, Yi Liu, Stéphane Gourguechon, Ching C Wang, Ziyin Li

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  9. Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
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  15. Mass measurements during lymphocytic leukemia cell polyploidization decouple cell cycle- and cell size-dependent growth.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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

5 authors at 1 institution in 1 country.

Tai AnDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Yi LiuDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Stéphane GourguechonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA.
Ching C WangDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA.
Ziyin LiDepartment of Microbiology and Molecular Genetics, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX 77030, USA. Electronic address: ziyin.li@uth.tmc.edu.
University of California, San Francisco · US

Funding

Mechanisms Of The Unusual Cytokinesis In TrypanosomesR01AI101437 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2013 to 2025
$6.4M
REGULATION OF THE DEVELOPMENT OF TRYPANOSOMA BRUCEIR01AI021786 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WANG, CHING CHUNG · 1985 to 2012
$4.2M
Regulation of cell cycle transitions by cyclin-dependent kinase in trypanosomesR01AI118736 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2016 to 2025
$3.8M
NIAID NIH HHS R01 AI021786NIAID NIH HHS R01 AI101437NIAID NIH HHS R01 AI118736
6 · The paper itself

Abstract

Protein translation in eukaryotes is cell-cycle dependent, with translation rates more robust in G1 phase of the cell cycle than in mitosis. However, whether the fundamental cell-cycle control machinery directly activates protein translation during the G1/S cell-cycle transition remains unknown. Using the early divergent eukaryote Trypanosoma brucei as a model organism, we report that the G1 cyclin-dependent kinase CRK1 phosphorylates two translation initiation factors, eIF4E4 and PABP1, to promote the G1/S cell-cycle transition and global protein translation. Phosphorylation of eIF4E4 by CRK1 enhances binding to the m

Indexed as

Cell CycleProtein BiosynthesisCDC2 Protein KinaseCyclin-Dependent KinasesEukaryotic Initiation Factor-4EGuaninePhosphorylationPoly APoly(A)-Binding Protein IProtein BindingProtozoan ProteinsRNA CapsSubstrate SpecificityTrypanosoma brucei brucei7-methylguanineCDC2 Protein Kinasecrk1 protein,Trypanosoma bruceiCyclin-Dependent KinasesEukaryotic Initiation Factor-4EGuaninePoly APoly(A)-Binding Protein IProtozoan ProteinsRNA Caps

Identifiers

PMID30540951
PMCPMC6350937
OpenAlexW2904986382

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.