Evidence map›Paper›PMID 23949737›Full record

ArticleHistochemistry and cell biology2014

RNA-binding protein RBM8A (Y14) and MAGOH localize to centrosome in human A549 cells.

Yasuhito Ishigaki, Yuka Nakamura, Takanori Tatsuno, Mitsumasa Hashimoto, Kuniyoshi Iwabuchi, Naohisa Tomosugi

Abstract read
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Article in Histochemistry and cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-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

18 citing papers in PubMed, 30 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Yasuhito IshigakiMedical Research Institute, Kanazawa Medical University, 1-1 Daigaku, Uchinada-machi, Kahoku, 920-0293, Japan, ishigaki@kanazawa-med.ac.jp.
Yuka Nakamura
Takanori Tatsuno
Mitsumasa Hashimoto
Kuniyoshi Iwabuchi
Naohisa Tomosugi
Kanazawa Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RBM8A (Y14) is carrying RNA-binding motif and forms the tight heterodimer with MAGOH. The heterodimer is known to be a member of exon junction complex on exporting mRNA and is required for mRNA metabolisms such as splicing, mRNA export and nonsense-mediated mRNA decay. Almost all RBM8A-MAGOH complexes localize in nucleoplasm and shuttle between nuclei and cytoplasm for RNA metabolism. Recently, the abnormality of G2/M transition and aberrant centrosome regulation in RBM8A- or MAGOH-deficient cells has been reported. These results prompt us to the reevaluation of the localization of RBM8A-MAGOH in human cells. Interestingly, our immunostaining experiments showed the localization of these proteins in centrosome in addition to nuclei. Furthermore, the transiently expressed eYFP-tagged RBM8A and Flag-tagged MAGOH also co-localized with centrosome signals. In addition, the proximity ligation in situ assay was performed to detect the complex formation in centrosome. Our experiments clearly showed that Myc-tagged RBM8A and Flag-tagged MAGOH formed a complex in centrosome. GFP-tagged PLK1 also co-localized with Myc-RBM8A. Our results show that RBM8A-MAGOH complex is required for M-phase progression via direct localization to centrosome rather than indirect effect.

Indexed as

Active Transport, Cell NucleusCell DivisionCell LineCell NucleusCentrosomeGreen Fluorescent ProteinsHumansNuclear ProteinsRNA-Binding ProteinsRNA, MessengerGreen Fluorescent ProteinsMAGOH protein, humanNuclear ProteinsRBM8A protein, humanRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID23949737
OpenAlexW2081631532

What OpenQuestion holds

Textmetadata
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.