Evidence map›Paper›PMID 31537859›Full record

ArticleScientific reports2019

The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase.

Kristyna Sala, Agnese Corbetta, Claudia Minici, Diletta Tonoli, David H Murray, Eugenia Cammarota, Lucrezia Ribolla, Martina Ramella, Riccardo Fesce, Davide Mazza and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

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  11. Liquid-liquid phase separation in synaptopathies.Neuroprotection (Chichester, England) · 2023
    Review
  12. Dengue virus NS5 degrades ERC1 during infection to antagonize NF-kB activation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

12 authors at 4 institutions in 2 countries.

Kristyna SalaDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy.
Agnese CorbettaDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy.
Claudia MiniciDivision of Immunology, Transplantation and Infectious Diseases, San Raffaele Scientific Institute, 20132, Milano, Italy.ORCID http://orcid.org/0000-0002-8350-484X
Diletta TonoliDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy.
David H MurrayDivision of Cell and Developmental Biology, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Eugenia CammarotaExperimental Imaging Center, San Raffaele Scientific Institute, 20132, Milano, Italy.
Lucrezia RibollaDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy.
Martina RamellaDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy.
Riccardo FesceHumanitas University, 20090, Pieve Emanuele, Italy.
Davide MazzaExperimental Imaging Center, San Raffaele Scientific Institute, 20132, Milano, Italy.
Massimo DeganoDivision of Immunology, Transplantation and Infectious Diseases, San Raffaele Scientific Institute, 20132, Milano, Italy.ORCID http://orcid.org/0000-0002-0787-1883
Ivan de CurtisDivision of Neuroscience, San Raffaele Scientific Institute and Vita-Salute San Raffaele University, 20132, Milano, Italy. decurtis.ivan@hsr.it.
Vita-Salute San Raffaele University · ITSan Raffaele University of Rome · ITHumanitas University · ITUniversity of Dundee · GB

Funding

Wellcome Trust 211193/Z/18/Z
6 · The paper itself

Abstract

Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell Line, TumorCell MembraneCell MovementChlorocebus aethiopsCOS CellsCytoplasmHumansNerve Tissue ProteinsNuclear Matrix-Associated Proteinsrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingErc1 protein, mouseNerve Tissue ProteinsNuclear Matrix-Associated Proteinsrab GTP-Binding Proteins

Identifiers

PMID31537859
PMCPMC6753080
OpenAlexW2973542976

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.