Evidence map›Paper›PMID 29615809›Full record

ArticleScientific reports2018

TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions.

Hye-Ran Kim, Min-Sung Kwon, Sangmin Lee, YeVin Mun, Kyung-Sik Lee, Chang-Hyun Kim, Bo-Ra Na, Bit Na Rae Kim, Indre Piragyte, Hyun-Su Lee and 6 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

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  12. Transgelin-2: A Double-Edged Sword in Immunity and Cancer Metastasis.Frontiers in cell and developmental biology · 2021
    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

16 authors at 5 institutions in 2 countries.

Hye-Ran KimSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Min-Sung KwonSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Sangmin LeeDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea.
YeVin MunSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Kyung-Sik LeeSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Chang-Hyun KimSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Bo-Ra NaSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Bit Na Rae KimSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Indre PiragyteSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Hyun-Su LeeSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Youngsoo JunSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Mi Sun JinSchool of Life Sciences, GIST, Gwangju, 61005, Korea.
Young-Min HyunDepartment of Anatomy, Yonsei University College of Medicine, Seoul, 03722, Korea.
Hyun Suk JungDepartment of Biochemistry, College of Natural Sciences, Kangwon National University, 1, Kangwondaehak-gil, Chuncheon-si, Gangwon-do, 24341, Korea.
Ji Young MunDepartment of Biomedical Laboratory Science, College of Health Science, Eulji University, Seongnam-si, Gyeonggi-do, 13135, Korea. mjy1026@gmail.com.
Chang-Duk JunSchool of Life Sciences, GIST, Gwangju, 61005, Korea. cdjun@gist.ac.kr.
Gwangju Institute of Science and Technology · KRShanghai Cell Therapy Research Institute · CNKangwon National University · KREulji University · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TAGLN is an actin-binding protein family that comprises three isoforms with theorized roles in smooth muscle differentiation, tumour development, lymphocyte activation, and brain chemistry. However, their fundamental characteristics in regulation of the actin-based cytoskeleton are not fully understood. Here we show that TAGLN2 (including TAGLN1 and TAGLN3) extensively nucleates G-actin polymerization under low-salt conditions, where polymerization would be completely suppressed. The calponin homology domain and actin-binding loop are essential to mechanically connect two adjacent G-actins, thereby mediating multimeric interactions. However, TAGLN2 blocked the Arp2/3 complex binding to actin filaments under physiological salt conditions, thereby inhibiting branched actin nucleation. In HeLa and T cells, TAGLN2 enhanced filopodium-like membrane protrusion. Collectively, the dual functional nature of TAGLN2-G-actin polymerization and Arp2/3 complex inhibition-may account for the mechanisms of filopodia development at the edge of Arp2/3-rich lamellipodia in various cell types.

Indexed as

Protein MultimerizationActin-Related Protein 2-3 ComplexActinsAnimalsHeLa CellsHumansMiceMicrofilament ProteinsModels, MolecularMuscle ProteinsProtein Structure, QuaternaryProtein TransportPseudopodiaActin-Related Protein 2-3 ComplexActinsMicrofilament ProteinsMuscle ProteinsTagln2 protein, humanTagln2 protein, mouse

Identifiers

PMID29615809
PMCPMC5883021
OpenAlexW2801471226

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.