Evidence map›Paper›PMID 30108131›Full record

ArticleGenes & development2018

Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2.

Alexandra Zinoviev, Akanksha Goyal, Supriya Jindal, John LaCava, Anton A Komar, Marina V Rodnina, Christopher U T Hellen, Tatyana V Pestova

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Human Tissues Exhibit Diverse Composition of Translation Machinery.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. [Research advances in the pathogenesis and treatment of neurodegeneration with brain iron accumulation].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors at 5 institutions in 2 countries.

Alexandra ZinovievDepartment of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, New York 11203, USA.
Akanksha GoyalDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Supriya JindalCenter for Gene Regulation in Health and Disease, Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, Ohio 44115, USA.
John LaCavaLaboratory of Cellular and Structural Biology, The Rockefeller University, New York 10065, USA.
Anton A KomarCenter for Gene Regulation in Health and Disease, Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, Ohio 44115, USA.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Christopher U T HellenDepartment of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, New York 11203, USA.
Tatyana V PestovaDepartment of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, New York 11203, USA.
Cleveland State University · USMax Planck Institute for Biophysical Chemistry · DESUNY Downstate Health Sciences University · USRockefeller University · USState University of New York · US

Funding

TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
Mechanisms of eukaryotic translation and ribosome-associated mRNA surveillance and protein quality controlR35GM122602 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI TATYANA V PESTOVA · 2017 to 2026
$4.8M
Non-canonical mechanisms of translation of viral mRNAsR01AI123406 · NIAID · SUNY DOWNSTATE MEDICAL CENTER · PI HELLEN, CHRISTOPHER ULRICH TRISTRAM · 2016 to 2020
$3.1M
THE MECHANISMS OF EUKARYOTIC TRANSLATION TERMINATION AND RIBOSOMAL RECYCLINGR01GM080623 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI PESTOVA, TATYANA V · 2007 to 2015
$2.7M
Understanding the impact of disease causing mutations in FIXR15HL121779 · NHLBI · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2014 to 2014
$437k
NHLBI NIH HHS R15 HL121779NIAID NIH HHS R01 AI123406NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM080623NIGMS NIH HHS R35 GM122602
6 · The paper itself

Abstract

GTP-binding protein 1 (GTPBP1) and GTPBP2 comprise a divergent group of translational GTPases with obscure functions, which are most closely related to eEF1A, eRF3, and Hbs1. Although recent reports implicated GTPBPs in mRNA surveillance and ribosome-associated quality control, how they perform these functions remains unknown. Here, we demonstrate that GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner. It also stimulates exosomal degradation of mRNAs in elongation complexes. The kinetics of GTPBP1-mediated elongation argues against its functioning in elongation per se but supports involvement in mRNA surveillance. Thus, GTP hydrolysis by GTPBP1 is not followed by rapid peptide bond formation, suggesting that after hydrolysis, GTPBP1 retains aa-tRNA, delaying its accommodation in the A site. In physiological settings, this would cause ribosome stalling, enabling GTPBP1 to elicit quality control programs; e.g., by recruiting the exosome. GTPBP1 can also deliver deacylated tRNA to the A site, indicating that it might function via interaction with deacylated tRNA, which accumulates during stresses. Although GTPBP2's binding to GTP was stimulated by Phe-tRNA

Indexed as

Peptide Chain Elongation, TranslationalExosome Multienzyme Ribonuclease ComplexGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateHEK293 CellsHumansMonomeric GTP-Binding ProteinsRNA, MessengerRNA StabilityRNA, TransferExosome Multienzyme Ribonuclease ComplexGTP-Binding ProteinsGTPBP1 protein, humanGTPBP2 protein, humanGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateMonomeric GTP-Binding ProteinsRNA, MessengerRNA, Transfer80S ribosomeGTPBP1GTPBP2RNA exosometranslation elongationtrGTPase

Identifiers

PMID30108131
PMCPMC6120710
OpenAlexW2887641870

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.