Evidence map›Paper›PMID 31548610›Full record

ArticleNature cell biology2019

Ankyrin repeat-containing N-Ank proteins shape cellular membranes.

David Wolf, Sarah Ann Hofbrucker-MacKenzie, Maryam Izadi, Eric Seemann, Frank Steiniger, Lukas Schwintzer, Dennis Koch, Michael Manfred Kessels, Britta Qualmann

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Pooled it
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  10. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
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  11. EHBP1 Is Critically Involved in the Dendritic Arbor Formation and Is Coupled to Factors Promoting Actin Filament Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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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

9 authors at 1 institution in 1 country.

David WolfInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Sarah Ann Hofbrucker-MacKenzieInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Maryam IzadiInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Eric SeemannInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Frank SteinigerElectron Microscopy Centre, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Lukas SchwintzerInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Dennis KochInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany.
Michael Manfred KesselsInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany. Michael.Kessels@med.uni-jena.de.ORCID http://orcid.org/0000-0001-5967-0744
Britta QualmannInstitute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, Jena, Germany. Britta.Qualmann@med.uni-jena.de.ORCID http://orcid.org/0000-0002-5743-5764
Jena University Hospital · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells of multicellular organisms need to adopt specific morphologies. However, the molecular mechanisms bringing about membrane topology changes are far from understood-mainly because knowledge of membrane-shaping proteins that can promote local membrane curvatures is still limited. Our analyses unveiled that several members of a large, previously unrecognised protein family, which we termed N-Ank proteins, use a combination of their ankyrin repeat array and an amino (N)-terminal amphipathic helix to bind and shape membranes. Consistently, functional analyses revealed that the N-Ank protein ankycorbin (NORPEG/RAI14), which was exemplarily characterised further, plays an important, ankyrin repeat-based and N-terminal amphipathic helix-dependent role in early morphogenesis of neurons. This function furthermore required coiled coil-mediated self-assembly and manifested as ankycorbin nanodomains marked by protrusive membrane topologies. In summary, here, we unveil a class of powerful membrane shapers and thereby assign mechanistic and cell biological functions to the N-Ank protein superfamily.

Indexed as

MorphogenesisAnimalsAnkyrin RepeatCell MembraneCells, CulturedCytoskeletal ProteinsHEK293 CellsHeLa CellsHumansMiceModels, MolecularNeuronsProtein DomainsRatsTranscription FactorsCytoskeletal ProteinsRai14 protein, mouseTranscription Factors

Identifiers

PMID31548610
OpenAlexW2974109588

What OpenQuestion holds

Textmetadata
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.