Evidence map›Paper›PMID 31182645›Full record

ArticleJournal of cell science2019

A trap mutant reveals the physiological client spectrum of TRC40.

Javier Coy-Vergara, Jhon Rivera-Monroy, Henning Urlaub, Christof Lenz, Blanche Schwappach

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

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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.

Javier Coy-VergaraDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen 37073, Germany.ORCID 0000-0002-4277-1618
Jhon Rivera-MonroyDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen 37073, Germany.ORCID 0000-0002-6911-9988
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.ORCID 0000-0003-1837-5233
Christof LenzBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.ORCID 0000-0002-0946-8166
Blanche SchwappachDepartment of Molecular Biology, University Medical Center Göttingen, Göttingen 37073, Germany blanche.schwappach@med.uni-goettingen.de.ORCID 0000-0003-0225-6432
Universitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane recognition complex (TRC) pathway targets tail-anchored (TA) proteins to the membrane of the endoplasmic reticulum (ER). While many TA proteins are known to be able to use this pathway, it is essential for the targeting of only a few. Here, we uncover a large number of TA proteins that engage with TRC40 when other targeting machineries are fully operational. We use a dominant-negative ATPase-impaired mutant of TRC40 in which aspartate 74 was replaced by a glutamate residue to trap TA proteins in the cytoplasm. Manipulation of the hydrophobic TA-binding groove in TRC40 (also known as ASNA1) reduces interaction with most, but not all, substrates suggesting that co-purification may also reflect interactions unrelated to precursor protein targeting. We confirm known TRC40 substrates and identify many additional TA proteins interacting with TRC40. By using the trap approach in combination with quantitative mass spectrometry, we show that Golgi-resident TA proteins such as the golgins golgin-84, CASP and giantin as well as the vesicle-associated membrane-protein-associated proteins VAPA and VAPB interact with TRC40. Thus, our results provide new avenues to assess the essential role of TRC40 in metazoan organisms.This article has an associated First Person interview with the first author of the paper.

Indexed as

Arsenite Transporting ATPasesCytoplasmGene SilencingHeLa CellsHumansHydrophobic and Hydrophilic InteractionsModels, BiologicalMutationProtein BindingSubcellular FractionsSubstrate SpecificityArsenite Transporting ATPasesGET3 protein, humanChaperoneClient spectrumEndoplasmic reticulumMembrane targetingTail-anchored proteinTRC40

Identifiers

PMID31182645
PMCPMC6633398
OpenAlexW2951084365

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.