Evidence map›Paper›PMID 31727776›Full record

ArticleThe Journal of cell biology2020

NuMA1 promotes axon initial segment assembly through inhibition of endocytosis.

Tomohiro Torii, Yuki Ogawa, Cheng-Hsin Liu, Tammy Szu-Yu Ho, Hamdan Hamdan, Chih-Chuan Wang, Juan A Oses-Prieto, Alma L Burlingame, Matthew N Rasband

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 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
1.8field-weighted citation impact, top 16% 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, 42 citations in OpenAlex.

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  18. α-Synuclein Promotes Neuronal Dysfunction and Death by Disrupting the Binding of Ankyrin to β-Spectrin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Tomohiro ToriiDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Yuki OgawaDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Cheng-Hsin LiuDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Tammy Szu-Yu HoDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Hamdan HamdanDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Chih-Chuan WangDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Juan A Oses-PrietoDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA.
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA.
Matthew N RasbandDepartment of Neuroscience, Baylor College of Medicine, Houston, TX.
Baylor College of Medicine · USUniversity of California, San Francisco · US

Funding

Neuroglial Interactions at the Node of RanvierR01NS044916 · NINDS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI RASBAND, MATTHEW N · 2002 to 2020
$4.2M
Mechanisms of CNS node of Ranvier formation.R01NS069688 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI RASBAND, MATTHEW N · 2010 to 2019
$3.4M
Neuroglial interactions at the node of RanvierR37NS044916 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI RASBAND, MATTHEW N · 2012 to 2018
$2.9M
NINDS NIH HHS R01 NS044916NINDS NIH HHS R01 NS069688NINDS NIH HHS R37 NS044916
6 · The paper itself

Abstract

Axon initial segments (AISs) initiate action potentials and regulate the trafficking of vesicles between somatodendritic and axonal compartments. However, the mechanisms controlling AIS assembly remain poorly defined. We performed differential proteomics and found nuclear mitotic apparatus protein 1 (NuMA1) is downregulated in AIS-deficient neonatal mouse brains and neurons. NuMA1 is transiently located at the AIS during development where it interacts with the scaffolding protein 4.1B and the dynein regulator lissencephaly 1 (Lis1). Silencing NuMA1 or protein 4.1B by shRNA disrupts AIS assembly, but not maintenance. Silencing Lis1 or overexpressing NuMA1 during AIS assembly increased the density of AIS proteins, including ankyrinG and neurofascin-186 (NF186). NuMA1 inhibits the endocytosis of AIS NF186 by impeding Lis1's interaction with doublecortin, a potent facilitator of NF186 endocytosis. Our results indicate the transient expression and AIS localization of NuMA1 stabilizes the developing AIS by inhibiting endocytosis and removal of AIS proteins.

Indexed as

Proteomics1-Alkyl-2-acetylglycerophosphocholine EsteraseAnimalsAnkyrinsAxon Initial SegmentAxonsCell Adhesion MoleculesCell Cycle ProteinsCytoskeletonDyneinsEndocytosisGene Expression RegulationHumansMiceMicrofilament ProteinsMicrotubule-Associated Proteins1-Alkyl-2-acetylglycerophosphocholine EsteraseAnk3 protein, mouseAnkyrinsCell Adhesion MoleculesCell Cycle ProteinsDyneinsEpb41l3 protein, mouseMicrofilament ProteinsMicrotubule-Associated ProteinsNerve Growth FactorsNfasc protein, mouseNuma1 protein, mousePafah1b1 protein, mouseRNA, Small Interfering

Identifiers

PMID31727776
PMCPMC7041696
OpenAlexW2983957605

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.