Evidence map›Paper›PMID 37597513›Full record

ArticleMolecular cell2023

A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.

Alexander J McQuown, Anjali R Nelliat, Dvir Reif, Ibrahim M Sabbarini, Britnie Santiago Membreno, Colin Chih-Chien Wu, Vladimir Denic

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. From metabolic dysregulation to malignancy: the presence ofJournal of gastrointestinal oncology · 2026
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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 3 institutions in 1 country.

Alexander J McQuownDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Anjali R NelliatDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Dvir ReifDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Ibrahim M SabbariniDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Britnie Santiago MembrenoRNA Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Colin Chih-Chien WuRNA Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Vladimir DenicDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. Electronic address: vdenic@mcb.harvard.edu.
Harvard University · USCenter for Cancer Research · USNational Cancer Institute · US

Funding

Mechanistic dissection of eukaryotic protein biogenesis and degradation pathwaysR35GM127136 · NIGMS · HARVARD UNIVERSITY · PI Vladimir Denic · 2018 to 2026
$5.0M
NIGMS NIH HHS R35 GM127136
6 · The paper itself

Abstract

General protein folding is mediated by chaperones that utilize ATP hydrolysis to regulate client binding and release. Zinc-finger protein 1 (Zpr1) is an essential ATP-independent chaperone dedicated to the biogenesis of eukaryotic translation elongation factor 1A (eEF1A), a highly abundant GTP-binding protein. How Zpr1-mediated folding is regulated to ensure rapid Zpr1 recycling remains an unanswered question. Here, we use yeast genetics and microscopy analysis, biochemical reconstitution, and structural modeling to reveal that folding of eEF1A by Zpr1 requires GTP hydrolysis. Furthermore, we identify the highly conserved altered inheritance of mitochondria 29 (Aim29) protein as a Zpr1 co-chaperone that recognizes eEF1A in the GTP-bound, pre-hydrolysis conformation. This interaction dampens Zpr1⋅eEF1A GTPase activity and facilitates client exit from the folding cycle. Our work reveals that a bespoke ATP-independent chaperone system has mechanistic similarity to ATPase chaperones but unexpectedly relies on client GTP hydrolysis to regulate the chaperone-client interaction.

Indexed as

Carrier ProteinsGTP PhosphohydrolasesMolecular ChaperonesPeptide Elongation FactorsSaccharomyces cerevisiae ProteinsAdenosine TriphosphateGuanosine TriphosphateHumansProtein FoldingSaccharomyces cerevisiaeAdenosine TriphosphateCarrier ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMolecular ChaperonesPeptide Elongation FactorsSaccharomyces cerevisiae ProteinsZPR1 protein, S cerevisiaechaperoneseEF1Aheat-shock responseintegrated stress responseprotein foldingprotein homeostasisproteostasistranslation elongation factors

Identifiers

PMID37597513
PMCPMC10528422
OpenAlexW4385978037

What OpenQuestion holds

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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.