Evidence map›Paper›PMID 35762204›Full record

ArticleeLife2022

CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre through phase separation.

Tsuyoshi Imasaki, Satoshi Kikkawa, Shinsuke Niwa, Yumiko Saijo-Hamano, Hideki Shigematsu, Kazuhiro Aoyama, Kaoru Mitsuoka, Takahiro Shimizu, Mari Aoki, Ayako Sakamoto and 10 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

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  16. Mechanisms underlying spindle assembly and robustness.Nature reviews. Molecular cell biology · 2023
    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

20 authors at 6 institutions in 1 country.

Tsuyoshi Imasaki *Division of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0001-5462-1820
Satoshi Kikkawa *Division of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Shinsuke NiwaFrontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, Japan.
Yumiko Saijo-HamanoDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Hideki ShigematsuRIKEN SPring-8 Center, Hyogo, Japan.ORCID 0000-0003-3951-8651
Kazuhiro AoyamaMaterials and Structural Analysis, Thermo Fisher Scientific, Tokyo, Japan.
Kaoru MitsuokaResearch Center for Ultra-High Voltage Electron Microscopy, Osaka University, Osaka, Japan.ORCID 0000-0003-1782-675X
Takahiro ShimizuDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Mari AokiRIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Ayako SakamotoRIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Yuri TomabechiRIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Naoki SakaiRIKEN SPring-8 Center, Hyogo, Japan.
Mikako ShirouzuRIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.ORCID 0000-0002-7997-2149
Shinya TaguchiDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0002-9868-0651
Yosuke YamagishiDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Tomiyoshi SetsuDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Yoshiaki SakihamaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Eriko NittaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.
Masatoshi TakeichiRIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Ryo NittaDivision of Structural Medicine and Anatomy, Department of Physiology and Cell Biology, Kobe University Graduate School of Medicine, Kobe, Japan.ORCID 0000-0002-6537-9272
Kobe University · JPRIKEN Center for Biosystems Dynamics Research · JPSPring-8 · JPThermo Fisher Scientific (Japan) · JPThe University of Osaka · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules are dynamic polymers consisting of αβ-tubulin heterodimers. The initial polymerization process, called microtubule nucleation, occurs spontaneously via αβ-tubulin. Since a large energy barrier prevents microtubule nucleation in cells, the γ-tubulin ring complex is recruited to the centrosome to overcome the nucleation barrier. However, a considerable number of microtubules can polymerize independently of the centrosome in various cell types. Here, we present evidence that the minus-end-binding calmodulin-regulated spectrin-associated protein 2 (CAMSAP2) serves as a strong nucleator for microtubule formation by significantly reducing the nucleation barrier. CAMSAP2 co-condensates with αβ-tubulin via a phase separation process, producing plenty of nucleation intermediates. Microtubules then radiate from the co-condensates, resulting in aster-like structure formation. CAMSAP2 localizes at the co-condensates and decorates the radiating microtubule lattices to some extent. Taken together, these in vitro findings suggest that CAMSAP2 supports microtubule nucleation and growth by organizing a nucleation centre as well as by stabilizing microtubule intermediates and growing microtubules.

Indexed as

SpectrinTubulinMicrotubule-Associated ProteinsMicrotubule-Organizing CenterMicrotubulesMicrotubule-Associated ProteinsSpectrinTubulinCAMSAPcell biologycryo-EME. coliLLPSmicrotubulemolecular biophysicsmousenucleationstructural biologyTIRF

Identifiers

PMID35762204
PMCPMC9239687
OpenAlexW4283704454

What OpenQuestion holds

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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.