Evidence map›Paper›PMID 37258650›Full record

ArticleScientific reports2023

Effects of three microtubule-associated proteins (MAP2, MAP4, and Tau) on microtubules' physical properties and neurite morphology.

Kohei Nishida, Kosuke Matsumura, Miki Tamura, Takuto Nakamichi, Keiya Shimamori, Masahiro Kuragano, Arif Md Rashedul Kabir, Akira Kakugo, Susumu Kotani, Naoki Nishishita and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
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  14. The role of autoantibodies in Alzheimer's disease: Pathogenetic connections or epiphenomena?Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
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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

11 authors at 5 institutions in 1 country.

Kohei NishidaGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Kosuke MatsumuraGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Miki TamuraGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Takuto NakamichiGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Keiya ShimamoriGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Masahiro KuraganoGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan.
Arif Md Rashedul KabirFaculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
Akira KakugoDepartment of Physics, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan.
Susumu KotaniFaculty of Science, Kanagawa University, Kanagawa, 221-8686, Japan.
Naoki NishishitaRegenerative Medicine and Cell Therapy Laboratories, Kaneka Corporation, Kobe, 650-0047, Japan.
Kiyotaka TokurakuGraduate School of Engineering, Muroran Institute of Technology, Muroran, 050-8585, Japan. tokuraku@mmm.muroran-it.ac.jp.
Muroran Institute of Technology · JPHokkaido University · JPKanagawa University · JPKaneka (Japan) · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The physical properties of cytoskeletal microtubules have a multifaceted effect on the expression of their cellular functions. A superfamily of microtubule-associated proteins, MAP2, MAP4, and tau, promote the polymerization of microtubules, stabilize the formed microtubules, and affect the physical properties of microtubules. Here, we show differences in the effects of these three MAPs on the physical properties of microtubules. When microtubule-binding domain fragments of MAP2, tau, and three MAP4 isoforms were added to microtubules in vitro and observed by fluorescence microscopy, tau-bound microtubules showed a straighter morphology than the microtubules bound by MAP2 and the three MAP4 isoforms. Flexural rigidity was evaluated by the shape of the teardrop pattern formed when microtubules were placed in a hydrodynamic flow, revealing that tau-bound microtubules were the least flexible. When full-length MAPs fused with EGFP were expressed in human neuroblastoma (SH-SY5Y) cells, the microtubules in apical regions of protrusions expressing tau were straighter than in cells expressing MAP2 and MAP4. On the other hand, the protrusions of tau-expressing cells had the fewest branches. These results suggest that the properties of microtubules, which are regulated by MAPs, contribute to the morphogenesis of neurites.

Indexed as

Microtubule-Associated ProteinsNeuroblastomaHumansMicrotubulesNeuritesProtein Bindingtau ProteinsMAP2 protein, humanMAP4 protein, humanMicrotubule-Associated Proteinstau Proteins

Identifiers

PMID37258650
PMCPMC10232483
OpenAlexW4378902712

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.