Evidence map›Paper›PMID 37477900›Full record

ArticleThe Journal of cell biology2023

ER-localized Shr3 is a selective co-translational folding chaperone necessary for amino acid permease biogenesis.

Ioanna Myronidi, Andreas Ring, Fei Wu, Per O Ljungdahl

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

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

4 authors at 1 institution in 1 country.

Ioanna Myronidi *Department of Molecular Biosciences, The Wenner-Gren Institute, SciLifeLab, Stockholm University, Stockholm, Sweden.ORCID 0009-0002-3935-7886
Andreas Ring *Department of Molecular Biosciences, The Wenner-Gren Institute, SciLifeLab, Stockholm University, Stockholm, Sweden.ORCID 0009-0005-7590-827X
Fei WuDepartment of Biochemistry and Biophysics, SciLifeLab, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-0120-7586
Per O LjungdahlDepartment of Molecular Biosciences, The Wenner-Gren Institute, SciLifeLab, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-6625-3540
Stockholm University · SE

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
NIGMS NIH HHS R01 GM129325
6 · The paper itself

Abstract

Proteins with multiple membrane-spanning segments (MS) co-translationally insert into the endoplasmic reticulum (ER) membrane of eukaryotic cells. Shr3, an ER membrane-localized chaperone in Saccharomyces cerevisiae, is required for the functional expression of a family of 18 amino acid permeases (AAP) comprised of 12 MS. We have used comprehensive scanning mutagenesis and deletion analysis of Shr3 combined with a modified split-ubiquitin approach to probe chaperone-substrate interactions in vivo. Shr3 selectively interacts with nested C-terminal AAP truncations in marked contrast to similar truncations of non-Shr3 substrate sugar transporters. Shr3-AAP interactions initiate with the first four MS of AAP and successively strengthen but weaken abruptly when all 12 MS are present. Shr3-AAP interactions are based on structural rather than sequence-specific interactions involving membrane and luminal domains of Shr3. The data align with Shr3 engaging nascent N-terminal chains of AAP, functioning as a scaffold to facilitate folding as translation completes.

Indexed as

Endoplasmic ReticulumSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino Acid Transport SystemsBiological TransportMolecular ChaperonesProtein FoldingSaccharomyces cerevisiaeAmino Acid Transport SystemsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSHR3 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID37477900
PMCPMC10359922
OpenAlexW4384924814

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.