Evidence map›Paper›PMID 36702972›Full record

ArticleNature structural & molecular biology2023

EGOC inhibits TOROID polymerization by structurally activating TORC1.

Manoël Prouteau, Clélia Bourgoint, Jan Felix, Lenny Bonadei, Yashar Sadian, Caroline Gabus, Savvas N Savvides, Irina Gutsche, Ambroise Desfosses, Robbie Loewith

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Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

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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

10 authors.

Manoël Prouteau *Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland. manoel.prouteau@unige.ch.ORCID 0000-0003-0076-2569
Clélia Bourgoint *Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.ORCID 0000-0002-1604-613X
Jan Felix *Unit for Structural Biology, Department of Biochemistry and Microbiology, Ghent University, Ghent, Belgium. Jan.Felix@UGent.be.ORCID 0000-0002-8436-9467
Lenny Bonadei *Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Yashar SadianCryoGEnic facility (DCI Geneva), University of Geneva, Geneva, Switzerland.
Caroline GabusDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Savvas N SavvidesUnit for Structural Biology, Department of Biochemistry and Microbiology, Ghent University, Ghent, Belgium.ORCID 0000-0003-3420-5947
Irina GutscheInstitut de Biologie Structurale, Université Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID 0000-0002-1908-3921
Ambroise DesfossesInstitut de Biologie Structurale, Université Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.ORCID 0000-0002-6525-5042
Robbie LoewithDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland. robbie.loewith@unige.ch.ORCID 0000-0002-2482-603X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Target of rapamycin complex 1 (TORC1) is a protein kinase controlling cell homeostasis and growth in response to nutrients and stresses. In Saccharomyces cerevisiae, glucose depletion triggers a redistribution of TORC1 from a dispersed localization over the vacuole surface into a large, inactive condensate called TOROID (TORC1 organized in inhibited domains). However, the mechanisms governing this transition have been unclear. Here, we show that acute depletion and repletion of EGO complex (EGOC) activity is sufficient to control TOROID distribution, independently of other nutrient-signaling pathways. The 3.9-Å-resolution structure of TORC1 from TOROID cryo-EM data together with interrogation of key interactions in vivo provide structural insights into TORC1-TORC1' and TORC1-EGOC interaction interfaces. These data support a model in which glucose-dependent activation of EGOC triggers binding to TORC1 at an interface required for TOROID assembly, preventing TORC1 polymerization and promoting release of active TORC1.

Indexed as

Saccharomyces cerevisiae ProteinsGlucoseMechanistic Target of Rapamycin Complex 1PolymerizationSaccharomyces cerevisiaeTranscription FactorsGlucoseMechanistic Target of Rapamycin Complex 1Saccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID36702972
PMCPMC10023571

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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.