Evidence map›Paper›PMID 24523293›Full record

ArticleMolecular biology of the cell2014

ER sheet persistence is coupled to myosin 1c-regulated dynamic actin filament arrays.

Merja Joensuu, Ilya Belevich, Olli Rämö, Ilya Nevzorov, Helena Vihinen, Maija Puhka, Tomasz M Witkos, Martin Lowe, Maria K Vartiainen, Eija Jokitalo

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 74 citations in OpenAlex.

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  4. Actin cytoskeleton and associated myosin motors within the renal epithelium.American journal of physiology. Renal physiology · 2024
    Review
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  9. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
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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 at 2 institutions in 2 countries.

Merja JoensuuCell and Molecular Biology Program, Institute of Biotechnology, 00014 University of Helsinki, Helsinki, Finland Electron Microscopy Unit, Institute of Biotechnology, 00014 University of Helsinki, Helsinki, Finland Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, United Kingdom.
Ilya Belevich
Olli Rämö
Ilya Nevzorov
Helena Vihinen
Maija Puhka
Tomasz M Witkos
Martin Lowe
Maria K Vartiainen
Eija Jokitalo
University of Helsinki · FIUniversity of Manchester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) comprises a dynamic three-dimensional (3D) network with diverse structural and functional domains. Proper ER operation requires an intricate balance within and between dynamics, morphology, and functions, but how these processes are coupled in cells has been unclear. Using live-cell imaging and 3D electron microscopy, we identify a specific subset of actin filaments localizing to polygons defined by ER sheets and tubules and describe a role for these actin arrays in ER sheet persistence and, thereby, in maintenance of the characteristic network architecture by showing that actin depolymerization leads to increased sheet fluctuation and transformations and results in small and less abundant sheet remnants and a defective ER network distribution. Furthermore, we identify myosin 1c localizing to the ER-associated actin filament arrays and reveal a novel role for myosin 1c in regulating these actin structures, as myosin 1c manipulations lead to loss of the actin filaments and to similar ER phenotype as observed after actin depolymerization. We propose that ER-associated actin filaments have a role in ER sheet persistence regulation and thus support the maintenance of sheets as a stationary subdomain of the dynamic ER network.

Indexed as

Actin CytoskeletonActinsCell Line, TumorEndoplasmic ReticulumHumansMicrotubulesMyosin Type IPhenotypePolymerizationProtein BindingProtein Structure, TertiaryStructure-Activity RelationshipActinsMYO1C protein, humanMyosin Type I

Identifiers

PMID24523293
PMCPMC3967974
OpenAlexW2143348982

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.