Evidence map›Paper›PMID 32344377›Full record

ArticleiScience2020

Tropomyosin Tpm3.1 Is Required to Maintain the Structure and Function of the Axon Initial Segment.

Amr Abouelezz, Holly Stefen, Mikael Segerstråle, David Micinski, Rimante Minkeviciene, Lauri Lahti, Edna C Hardeman, Peter W Gunning, Casper C Hoogenraad, Tomi Taira and 2 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

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  19. The role of the membrane-associated periodic skeleton in axons.Cellular and molecular life sciences : CMLS · 2021
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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 5 institutions in 3 countries.

Amr AbouelezzMinerva Foundation Institute for Medical Research, Biomedicum Helsinki 2U, Tukholmankatu 8, 00290 Helsinki, Finland; HiLIFE - Neuroscience Center, University of Helsinki, Haartmaninkatu 8, 00290 Helsinki, Finland.
Holly StefenSchool of Medical Sciences, UNSW Sydney, Sydney, NSW 2052, Australia.
Mikael SegerstråleFaculty of Biological and Environmental Sciences, University of Helsinki, Viikinkaari 1, 00790 Helsinki, Finland.
David MicinskiMinerva Foundation Institute for Medical Research, Biomedicum Helsinki 2U, Tukholmankatu 8, 00290 Helsinki, Finland.
Rimante MinkevicieneMinerva Foundation Institute for Medical Research, Biomedicum Helsinki 2U, Tukholmankatu 8, 00290 Helsinki, Finland.
Lauri LahtiDepartment of Computer Science, Aalto University School of Science, Espoo, Finland.
Edna C HardemanSchool of Medical Sciences, UNSW Sydney, Sydney, NSW 2052, Australia.
Peter W GunningSchool of Medical Sciences, UNSW Sydney, Sydney, NSW 2052, Australia.
Casper C HoogenraadCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584CH Utrecht, the Netherlands.
Tomi TairaFaculty of Veterinary Medicine, University of Helsinki, Agnes Sjöbergin katu 2, 00790 Helsinki, Finland.
Thomas FathSchool of Medical Sciences, UNSW Sydney, Sydney, NSW 2052, Australia; Dementia Research Centre, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, NSW 2109, Australia.
Pirta HotulainenMinerva Foundation Institute for Medical Research, Biomedicum Helsinki 2U, Tukholmankatu 8, 00290 Helsinki, Finland. Electronic address: pirta.hotulainen@helsinki.fi.
Minerva Foundation · FIUNSW Sydney · AUUniversity of Helsinki · FIAalto University · FIUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The axon initial segment (AIS) is the site of action potential initiation and serves as a cargo transport filter and diffusion barrier that helps maintain neuronal polarity. The AIS actin cytoskeleton comprises actin patches and periodic sub-membranous actin rings. We demonstrate that tropomyosin isoform Tpm3.1 co-localizes with actin patches and that the inhibition of Tpm3.1 led to a reduction in the density of actin patches. Furthermore, Tpm3.1 showed a periodic distribution similar to sub-membranous actin rings but Tpm3.1 was only partially congruent with sub-membranous actin rings. Nevertheless, the inhibition of Tpm3.1 affected the uniformity of the periodicity of actin rings. Furthermore, Tpm3.1 inhibition led to reduced accumulation of AIS structural and functional proteins, disruption in sorting somatodendritic and axonal proteins, and a reduction in firing frequency. These results show that Tpm3.1 is necessary for the structural and functional maintenance of the AIS.

Indexed as

Biological SciencesCell BiologyCellular NeuroscienceMolecular Neuroscience

Identifiers

PMID32344377
PMCPMC7186529
OpenAlexW3016092853

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.