Evidence map›Paper›PMID 33738926›Full record

ArticleEMBO reports2021

Hsp90-mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling.

Laura Mediani, Francesco Antoniani, Veronica Galli, Jonathan Vinet, Arianna Dorotea Carrà, Ilaria Bigi, Vadreenath Tripathy, Tatiana Tiago, Marco Cimino, Giuseppina Leo and 13 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 80 citations in OpenAlex.

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  9. Organization of the Proteostasis Network of Membraneless Organelles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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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

23 authors at 9 institutions in 4 countries.

Laura MedianiDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Francesco AntonianiDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Veronica GalliDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Jonathan VinetDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Arianna Dorotea CarràDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Ilaria BigiDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Vadreenath TripathyCenter for Regenerative Therapies TU Dresden, Technische Universität Dresden, Dresden, Germany.
Tatiana TiagoDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Marco CiminoDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Giuseppina LeoDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.
Triana AmenDepartment of Experimental Neurodegeneration, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-4808-7806
Daniel KaganovichDepartment of Experimental Neurodegeneration, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-2398-1596
Cristina CeredaGenomic and Post-Genomic Center, IRCCS Mondino Foundation, Pavia, Italy.ORCID 0000-0001-9571-0862
Orietta PansarasaGenomic and Post-Genomic Center, IRCCS Mondino Foundation, Pavia, Italy.
Jessica MandrioliDepartment of Neuroscience, St. Agostino Estense Hospital, Azienda Ospedaliero Universitaria di Modena, Modena, Italy.
Priyanka TripathiInstitute of Neuropathology, RWTH Aachen University Hospital, Aachen, Germany.
Dirk TroostDepartment of (Neuro)Pathology, Amsterdam Neuroscience, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Eleonora AronicaDepartment of (Neuro)Pathology, Amsterdam Neuroscience, Amsterdam UMC, University of Amsterdam, Amsterdam, The Netherlands.
Johannes BuchnerCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.ORCID 0000-0003-1282-7737
Anand GoswamiInstitute of Neuropathology, RWTH Aachen University Hospital, Aachen, Germany.
Jared SterneckertCenter for Regenerative Therapies TU Dresden, Technische Universität Dresden, Dresden, Germany.
Simon AlbertiBiotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universität Dresden, Dresden, Germany.ORCID 0000-0003-4017-6505
Serena CarraDepartment of Biomedical, Metabolic and Neural Sciences, Centre for Neuroscience and Nanotechnology, University of Modena and Reggio Emilia, Modena, Italy.ORCID 0000-0003-0939-0140
University of Modena and Reggio Emilia · ITAmsterdam Neuroscience · NLFoundation Center · USTechnische Universität Dresden · DEUniversitätsklinikum Aachen · DEUniversitätsmedizin Göttingen · DEAzienda Unita' Sanitaria Locale Di Modena · ITCenter for Integrated Protein Science Munich · DECenter for Systems Biology Dresden · DE

Funding

European Research Council ERC-StG2013 337713European Research Council (ERC) 725836
6 · The paper itself

Abstract

Stress granules (SGs) are dynamic condensates associated with protein misfolding diseases. They sequester stalled mRNAs and signaling factors, such as the mTORC1 subunit raptor, suggesting that SGs coordinate cell growth during and after stress. However, the molecular mechanisms linking SG dynamics and signaling remain undefined. We report that the chaperone Hsp90 is required for SG dissolution. Hsp90 binds and stabilizes the dual-specificity tyrosine-phosphorylation-regulated kinase 3 (DYRK3) in the cytosol. Upon Hsp90 inhibition, DYRK3 dissociates from Hsp90 and becomes inactive. Inactive DYRK3 is subjected to two different fates: it either partitions into SGs, where it is protected from irreversible aggregation, or it is degraded. In the presence of Hsp90, DYRK3 is active and promotes SG disassembly, restoring mTORC1 signaling and translation. Thus, Hsp90 links stress adaptation and cell growth by regulating the activity of a key kinase involved in condensate disassembly and translation restoration.

Indexed as

Cytoplasmic GranulesSignal TransductionCytoplasmMechanistic Target of Rapamycin Complex 1PhosphorylationRNA, MessengerMechanistic Target of Rapamycin Complex 1RNA, MessengerDYRK3FUS-ALSHsp90phase separationstress granules

Identifiers

PMID33738926
PMCPMC8097338
OpenAlexW3139318772

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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.