Evidence map›Paper›PMID 30190432›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

CAMSAP3 maintains neuronal polarity through regulation of microtubule stability.

Varisa Pongrakhananon, Hiroko Saito, Sylvain Hiver, Takaya Abe, Go Shioi, Wenxiang Meng, Masatoshi Takeichi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 83 citations in OpenAlex.

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  4. Tppp3 determines basal body positioning and identity of respiratory cilia via microtubule assembly and sphingolipid homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

7 authors at 2 institutions in 3 countries.

Varisa PongrakhananonLaboratory for Cell Adhesion and Tissue Patterning, RIKEN Center for Developmental Biology/RIKEN Center for Biosystems Dynamics Research, 650-0047 Kobe, Japan.
Hiroko SaitoLaboratory for Cell Adhesion and Tissue Patterning, RIKEN Center for Developmental Biology/RIKEN Center for Biosystems Dynamics Research, 650-0047 Kobe, Japan.
Sylvain HiverLaboratory for Cell Adhesion and Tissue Patterning, RIKEN Center for Developmental Biology/RIKEN Center for Biosystems Dynamics Research, 650-0047 Kobe, Japan.
Takaya AbeAnimal Resource Development Unit, RIKEN Center for Life Science Technologies, 650-0047 Kobe, Japan.
Go ShioiGenetic Engineering Team, RIKEN Center for Life Science Technologies, 650-0047 Kobe, Japan.
Wenxiang MengState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, 100101 Beijing, China.
Masatoshi TakeichiLaboratory for Cell Adhesion and Tissue Patterning, RIKEN Center for Developmental Biology/RIKEN Center for Biosystems Dynamics Research, 650-0047 Kobe, Japan; masatoshi.takeichi@riken.jp.
RIKEN Center for Biosystems Dynamics Research · JPInstitute of Genetics and Developmental Biology · CN

Funding

Wellcome Trust
6 · The paper itself

Abstract

The molecular mechanisms that guide each neuron to become polarized, forming a single axon and multiple dendrites, remain unknown. Here we show that CAMSAP3 (calmodulin-regulated spectrin-associated protein 3), a protein that regulates the minus-end dynamics of microtubules, plays a key role in maintaining neuronal polarity. In mouse hippocampal neurons, CAMSAP3 was enriched in axons. Although axonal microtubules were generally acetylated, CAMSAP3 was preferentially localized along a less-acetylated fraction of the microtubules. CAMSAP3-mutated neurons often exhibited supernumerary axons, along with an increased number of neurites having nocodazole-resistant/acetylated microtubules compared with wild-type neurons. Analysis using cell lines showed that CAMSAP3 depletion promoted tubulin acetylation, and conversely, mild overexpression of CAMSAP3 inhibited it, suggesting that CAMSAP3 works to retain nonacetylated microtubules. In contrast, CAMSAP2, a protein related to CAMSAP3, was detected along all neurites, and its loss did not affect neuronal polarity, nor did it cause increased tubulin acetylation. Depletion of α-tubulin acetyltransferase-1 (αTAT1), the key enzyme for tubulin acetylation, abolished CAMSAP3 loss-dependent multiple-axon formation. These observations suggest that CAMSAP3 sustains a nonacetylated pool of microtubules in axons, interfering with the action of αTAT1, and this process is important to maintain neuronal polarity.

Indexed as

Cell PolarityAcetylationAnimalsHippocampusMiceMice, KnockoutMicrotubule-Associated ProteinsMicrotubulesNeuronsTubulinCamsap3 protein, mouseMicrotubule-Associated ProteinsTubulinaxonCAMSAPmicrotubuleneuronal polarityαTAT1

Identifiers

PMID30190432
PMCPMC6166842
OpenAlexW2892150329

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.