Evidence map›Paper›PMID 21745818›Full record

ArticleNucleic acids research2011

Mechanisms of translational regulation by a human eIF5-mimic protein.

Chingakham Ranjit Singh, Ryosuke Watanabe, Donghui Zhou, Martin D Jennings, Akira Fukao, Bumjun Lee, Yuka Ikeda, John A Chiorini, Susan G Campbell, Mark P Ashe and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
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  4. Structural basis for non-AUG translation regulation by 5MPs.bioRxiv : the preprint server for biology · 2025
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  6. CriticalNAR genomics and bioinformatics · 2024
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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

14 authors at 4 institutions in 3 countries.

Chingakham Ranjit SinghMolecular Cellular and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Ryosuke Watanabe
Donghui Zhou
Martin D Jennings
Akira Fukao
Bumjun Lee
Yuka Ikeda
John A Chiorini
Susan G Campbell
Mark P Ashe
Toshinobu Fujiwara
Ronald C Wek
Graham D Pavitt
Katsura Asano
Kansas State University · USIndiana University Bloomington · USUniversity of Manchester · GBNational Institutes of Health · US

Funding

UNDERSTANDING THE ROLE OF SMALL RNAS IN ARABIDOPSIS POLLEN DEVELOPMENTP20RR016475 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ACKLEY, BRIAN DOUGLAS · 2001 to 2011
$38.1M
Adeno-associated Virus Biology And Utilization For Gene TransferZIADE000695 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI CHIORINI, JAY · 2009 to 2025
$36.6M
Metabolic stress responses andeIF2 kinase GCN2R01GM049164 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WEK, RONALD C · 1998 to 2019
$6.3M
Studies on start codon selection by eukaryotic ribosomesR01GM064781 · NIGMS · KANSAS STATE UNIVERSITY · PI ASANO, KATSURA · 2002 to 2010
$2.4M
HISRS-DOMAIN AND REGULATING GCN2 PROTEIN KINASER29GM049164 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WEK, RONALD C · 1993 to 1997
–
Biotechnology and Biological Sciences Research Council BB/E002005/1Biotechnology and Biological Sciences Research Council BB/H010599/1Intramural NIH HHSNCRR NIH HHS P20 RR016475NIGMS NIH HHS GM49164NIGMS NIH HHS GM64781NIGMS NIH HHS R01 GM049164
6 · The paper itself

Abstract

The translation factor eIF5 is an important partner of eIF2, directly modulating its function in several critical steps. First, eIF5 binds eIF2/GTP/Met-tRNA(i)(Met) ternary complex (TC), promoting its recruitment to 40S ribosomal subunits. Secondly, its GTPase activating function promotes eIF2 dissociation for ribosomal subunit joining. Finally, eIF5 GDP dissociation inhibition (GDI) activity can antagonize eIF2 reactivation by competing with the eIF2 guanine exchange factor (GEF), eIF2B. The C-terminal domain (CTD) of eIF5, a W2-type HEAT domain, mediates its interaction with eIF2. Here, we characterize a related human protein containing MA3- and W2-type HEAT domains, previously termed BZW2 and renamed here as eIF5-mimic protein 1 (5MP1). Human 5MP1 interacts with eIF2 and eIF3 and inhibits general and gene-specific translation in mammalian systems. We further test whether 5MP1 is a mimic or competitor of the GEF catalytic subunit eIF2Bε or eIF5, using yeast as a model. Our results suggest that 5MP1 interacts with yeast eIF2 and promotes TC formation, but inhibits TC binding to the ribosome. Moreover, 5MP1 is not a GEF but a weak GDI for yeast eIF2. We propose that 5MP1 is a partial mimic and competitor of eIF5, interfering with the key steps by which eIF5 regulates eIF2 function.

Indexed as

Gene Expression RegulationProtein BiosynthesisActivating Transcription Factor 4AnimalsCell LineDNA-Binding ProteinsEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-2BEukaryotic Initiation Factor-3Eukaryotic Initiation FactorsEukaryotic Translation Initiation Factor 5AGuanosine DiphosphateHeLa CellsHumansMiceMolecular MimicryActivating Transcription Factor 4BZW2 protein, humanDNA-Binding ProteinsEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-2BEukaryotic Initiation Factor-3Eukaryotic Initiation FactorsEukaryotic Translation Initiation Factor 5AGCN2 protein, S cerevisiaeGuanosine DiphosphatePeptide Initiation FactorsProtein Serine-Threonine KinasesRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21745818
PMCPMC3201852
OpenAlexW2077143031

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.