Evidence map›Paper›PMID 30224724›Full record

ArticleNature communications2018

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface.

Tobias Karlberg, Peter Hornyak, Ana Filipa Pinto, Stefina Milanova, Mahsa Ebrahimi, Mikael Lindberg, Nikolai Püllen, Axel Nordström, Elinor Löverli, Rémi Caraballo and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-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

27 citing papers in PubMed, 51 citations in OpenAlex.

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  7. Evidence for intracellularJournal of bacteriology · 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

17 authors at 4 institutions in 2 countries.

Tobias KarlbergDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Peter HornyakDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Ana Filipa PintoDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Stefina MilanovaDepartment of Cellular and Molecular Biology, Karolinska Institutet, Berzelius väg 35, 17165, Solna, Sweden.
Mahsa EbrahimiDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Mikael LindbergProtein Expertise Platform, Umeå University, Kemihuset, 90187, Umeå, Sweden.
Nikolai PüllenDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Axel NordströmDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.ORCID http://orcid.org/0000-0003-2314-3322
Elinor LöverliDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Rémi CaraballoDepartment of Chemistry, Umeå University, Kemihuset, 90187, Umeå, Sweden.
Emily V WongMolecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Katja NäreojaDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Ann-Gerd ThorsellDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.
Mikael ElofssonDepartment of Chemistry, Umeå University, Kemihuset, 90187, Umeå, Sweden.
Enrique M De La CruzMolecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.
Camilla BjörkegrenDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden.ORCID http://orcid.org/0000-0001-7354-9270
Herwig SchülerDepartment of Biosciences and Nutrition, Karolinska Institutet, Hälsovägen 4c, 14157, Huddinge, Sweden. herwig.schuler@ki.se.ORCID http://orcid.org/0000-0003-4059-3501
Karolinska Institutet · SEUmeå University · SEUniversity of California, San Francisco · USYale University · US

Funding

Actin filament elasticity and actin-binding protein functionR01GM097348 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2011 to 2018
$3.1M
National Science Foundation (NSF) DGE-1122492NIGMS NIH HHS R01 GM097348U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM097348Vetenskapsrådet (Swedish Research Council) 2012-2802
6 · The paper itself

Abstract

Pseudomonas are a common cause of hospital-acquired infections that may be lethal. ADP-ribosyltransferase activities of Pseudomonas exotoxin-S and -T depend on 14-3-3 proteins inside the host cell. By binding in the 14-3-3 phosphopeptide binding groove, an amphipathic C-terminal helix of ExoS and ExoT has been thought to be crucial for their activation. However, crystal structures of the 14-3-3β:ExoS and -ExoT complexes presented here reveal an extensive hydrophobic interface that is sufficient for complex formation and toxin activation. We show that C-terminally truncated ExoS ADP-ribosyltransferase domain lacking the amphipathic binding motif is active when co-expressed with 14-3-3. Moreover, swapping the amphipathic C-terminus with a fragment from Vibrio Vis toxin creates a 14-3-3 independent toxin that ADP-ribosylates known ExoS targets. Finally, we show that 14-3-3 stabilizes ExoS against thermal aggregation. Together, this indicates that 14-3-3 proteins activate exotoxin ADP-ribosyltransferase domains by chaperoning their hydrophobic surfaces independently of the amphipathic C-terminal segment.

Indexed as

14-3-3 ProteinsADP Ribose TransferasesBacterial ToxinsBinding SitesCrystallography, X-RayEscherichia coliGTPase-Activating ProteinsHost-Pathogen InteractionsHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular ChaperonesProtein ConformationProtein DomainsPseudomonas aeruginosaSaccharomyces cerevisiae14-3-3 ProteinsADP Ribose TransferasesBacterial Toxinsexoenzyme SExoT protein, Pseudomonas aeruginosaGTPase-Activating ProteinsMolecular Chaperones

Identifiers

PMID30224724
PMCPMC6141617
OpenAlexW2806534677

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.