Evidence map›Paper›PMID 28854361›Full record

ArticleCell reports2017

Aberrant Compartment Formation by HSPB2 Mislocalizes Lamin A and Compromises Nuclear Integrity and Function.

Federica F Morelli, Dineke S Verbeek, Jessika Bertacchini, Jonathan Vinet, Laura Mediani, Sandra Marmiroli, Giovanna Cenacchi, Milena Nasi, Sara De Biasi, Jeanette F Brunsting and 6 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Nuclear Proteome Map of Mouse Heart Chambers.Molecular & cellular proteomics : MCP · 2026
    Article
  2. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. Article
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  5. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Evaluation of the Small Heat Shock Protein Family MembersInternational journal of molecular sciences · 2023
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
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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

16 authors at 7 institutions in 4 countries.

Federica F MorelliDepartment of Biomedical, Metabolic and Neuronal Sciences, University of Modena and Reggio Emilia, and Center for Neuroscience and Neurotechnology, 41125 Modena, Italy.
Dineke S VerbeekDepartment of Genetics, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, the Netherlands.
Jessika BertacchiniDepartment of Biomedical, Metabolic and Neuronal Sciences, University of Modena and Reggio Emilia, and Center for Neuroscience and Neurotechnology, 41125 Modena, Italy.
Jonathan VinetDepartment of Biomedical, Metabolic and Neuronal Sciences, University of Modena and Reggio Emilia, and Center for Neuroscience and Neurotechnology, 41125 Modena, Italy.
Laura MedianiDepartment of Biomedical, Metabolic and Neuronal Sciences, University of Modena and Reggio Emilia, and Center for Neuroscience and Neurotechnology, 41125 Modena, Italy.
Sandra MarmiroliDepartment of Surgery, Medicine, Dentistry and Morphology, University of Modena and Reggio Emilia, 41125 Modena, Italy.
Giovanna CenacchiDepartment of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy.
Milena NasiDepartment of Surgery, Medicine, Dentistry and Morphology, University of Modena and Reggio Emilia, 41125 Modena, Italy.
Sara De BiasiDepartment of Surgery, Medicine, Dentistry and Morphology, University of Modena and Reggio Emilia, 41125 Modena, Italy.
Jeanette F BrunstingDepartment of Cell Biology, University of Groningen, University Medical Center Groningen, 9713 AV Groningen, the Netherlands.
Jan LammerdingMeinig School of Biomedical Engineering, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853-7202, USA.
Elena PegoraroDepartment of Neurosciences, University of Padua, 35122 Padua, Italy.
Corrado AngeliniIRCCS S. Camillo Hospital, 30126 Lido Venice, Italy.
Rossella TuplerDepartment of Life Sciences, University of Modena and Reggio Emilia, 41125 Modena, Italy.
Simon AlbertiMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Serena CarraDepartment of Biomedical, Metabolic and Neuronal Sciences, University of Modena and Reggio Emilia, and Center for Neuroscience and Neurotechnology, 41125 Modena, Italy. Electronic address: serena.carra@unimore.it.
University of Modena and Reggio Emilia · ITUniversity Medical Center Groningen · NLCornell University · USIRCCS San Camillo Hospital · ITMax Planck Institute of Molecular Cell Biology and Genetics · DEUniversity of Bologna · ITUniversity of Padua · IT

Funding

Nuclear mechanics and mechanotransduction in muscular laminopathiesR01HL082792 · NHLBI · CORNELL UNIVERSITY · PI LAMMERDING, JAN · 2007 to 2023
$4.8M
NHLBI NIH HHS R01 HL082792Telethon GGP15001
6 · The paper itself

Abstract

Small heat shock proteins (HSPBs) contain intrinsically disordered regions (IDRs), but the functions of these IDRs are still unknown. Here, we report that, in mammalian cells, HSPB2 phase separates to form nuclear compartments with liquid-like properties. We show that phase separation requires the disordered C-terminal domain of HSPB2. We further demonstrate that, in differentiating myoblasts, nuclear HSPB2 compartments sequester lamin A. Increasing the nuclear concentration of HSPB2 causes the formation of aberrant nuclear compartments that mislocalize lamin A and chromatin, with detrimental consequences for nuclear function and integrity. Importantly, phase separation of HSPB2 is regulated by HSPB3, but this ability is lost in two identified HSPB3 mutants that are associated with myopathy. Our results suggest that HSPB2 phase separation is involved in reorganizing the nucleoplasm during myoblast differentiation. Furthermore, these findings support the idea that aberrant HSPB2 phase separation, due to HSPB3 loss-of-function mutations, contributes to myopathy.

Indexed as

Cell CompartmentationAdultAmino Acid SequenceCell NucleusChromatinHeat-Shock ProteinsHeLa CellsHSP27 Heat-Shock ProteinsHumansLamin Type AMusclesMuscular DiseasesMutationMyogeninProtein TransportRNAChromatinHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB2 protein, humanHSPB3 protein, humanLamin Type AMyogeninRNAcongenital myopathylamin-A/Cnucleusphase transitionsmall HSPs

Identifiers

PMID28854361
PMCPMC5583511
OpenAlexW2751577001

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.