Evidence map›Paper›PMID 27734173›Full record

ArticleJournal of plant research2016

Plant Aurora kinases interact with and phosphorylate transcription factors.

Mai Takagi, Takuya Sakamoto, Ritsuko Suzuki, Keiichirou Nemoto, Takeshi Obayashi, Takeshi Hirakawa, Tomoko M Matsunaga, Daisuke Kurihara, Yuko Nariai, Takeshi Urano and 2 more

Abstract read
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Article in Journal of plant research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Functional Divergence of Microtubule-Associated TPX2 Family Members inInternational journal of molecular sciences · 2020
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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

12 authors at 5 institutions in 1 country.

Mai TakagiDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Takuya SakamotoDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Ritsuko SuzukiDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Keiichirou NemotoProteo-Science Center, Ehime University, Matsuyama, Ehime, 791-8577, Japan.
Takeshi ObayashiGraduate School of Information Sciences, Tohoku University, Sendai, Miyagi, 980-8679, Japan.
Takeshi HirakawaDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Tomoko M MatsunagaInstitute for Science and Technology, Tokyo University of Science, Noda, Chiba, 278-8510, Japan.
Daisuke KuriharaDivision of Biological Science, Graduate School of Science, Nagoya University, JST ERATO Higashiyama Live-Holonics Project, Furo-cho, Chikusa-ku, Nagoya, Aichi, 464-8602, Japan.
Yuko NariaiDepartment of Biochemistry, Faculty of Medicine, Shimane University, Izumo, Shimane, 693-8501, Japan.
Takeshi UranoDepartment of Biochemistry, Faculty of Medicine, Shimane University, Izumo, Shimane, 693-8501, Japan.
Tatsuya SawasakiProteo-Science Center, Ehime University, Matsuyama, Ehime, 791-8577, Japan.
Sachihiro MatsunagaDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. sachi@rs.tus.ac.jp.
Tokyo University of Science · JPEhime University · JPShimane University · JPNagoya University · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aurora kinase (AUR) is a well-known mitotic serine/threonine kinase that regulates centromere formation, chromosome segregation, and cytokinesis in eukaryotes. In addition to regulating mitotic events, AUR has been shown to regulate protein dynamics during interphase in animal cells. In contrast, there has been no identification and characterization of substrates and/or interacting proteins during interphase in plants. The Arabidopsis thaliana genome encodes three AUR paralogues, AtAUR1, AtAUR2, and AtAUR3. Among them, AtAUR1 and AtAUR2 are considered to function redundantly. Here, we confirmed that both AtAUR1 and AtAUR3 are localized in the nucleus and cytoplasm during interphase, suggesting that they have functions during interphase. To identify novel interacting proteins, we used AlphaScreen to target 580 transcription factors (TFs) that are mainly functional during interphase, using recombinant A. thaliana TFs and AtAUR1 or AtAUR3. We found 133 and 32 TFs had high potential for interaction with AtAUR1 and AtAUR3, respectively. The highly AtAUR-interacting TFs were involved in various biological processes, suggesting the functions of the AtAURs during interphase. We found that AtAUR1 and AtAUR3 showed similar interaction affinity to almost all TFs. However, in some cases, the interaction affinity differed substantially between the two AtAUR homologues. These results suggest that AtAUR1 and AtAUR3 have both redundant and distinct functions through interactions with TFs. In addition, database analysis revealed that most of the highly AtAUR-interacting TFs contained a detectable phosphopeptide that was consistent with the consensus motifs for human AURs, suggesting that these TFs are substrates of the AtAURs. The AtAURs phosphorylated several highly interacting TFs in the AlphaScreen in vitro. Overall, in line with the regulation of TFs through interaction, our results indicate the possibility of phosphoregulation of several TFs by the AtAURs (280/300).

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsInterphasePhosphorylationProtein Serine-Threonine KinasesTranscription FactorsArabidopsis ProteinsAUR1 protein, ArabidopsisAUR3 protein, ArabidopsisProtein Serine-Threonine KinasesTranscription FactorsAlphaScreenAurora kinaseIn vitro phosphorylation assay with ATPγSTranscription factorsWheat germ cell-free protein synthesis

Identifiers

PMID27734173
OpenAlexW2530141404

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.