Evidence map›Paper›PMID 21637952›Full record

ArticleMolecular biology reports2012

Plk1-mediated phosphorylation of UAP56 regulates the stability of UAP56.

Fuyin Xiong, Yanli Lin, Zhengbin Han, Gengshou Shi, Liyuan Tian, Xiaojie Wu, Qiangcheng Zeng, Yanrong Zhou, Jixian Deng, Hongxing Chen

Abstract read
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In one paragraph

Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

10 citing papers in PubMed, 15 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

10 authors at 2 institutions in 2 countries.

Fuyin XiongBeijing Institute of Biotechnology, Beijing 100071, People's Republic of China.
Yanli Lin
Zhengbin Han
Gengshou Shi
Liyuan Tian
Xiaojie Wu
Qiangcheng Zeng
Yanrong Zhou
Jixian Deng
Hongxing Chen
Beijing VDJBio (China) · CNCzech Academy of Sciences, Institute of Biotechnology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polo-like kinase 1 (Plk1) is a conserved serine/threonine protein kinase that plays pivotal roles during the cell cycle and cell proliferation. Although a number of important targets have been identified, the mechanism of Plk1-regulated pathways and the bulk of the Plk1 interactome are largely unknown. Here, we demonstrate that Plk1 interacts with the DExH/D RNA helicase, UAP56. The protein levels of UAP56 and Plk1 are inversely correlated during the cell cycle. We also show that Plk1 phosphorylates UAP56 in vitro and in vivo and that Plk1-dependent phosphorylation of UAP56 triggers ubiquitination and degradation of UAP56 through proteasomes. This result suggests that Plk1-mediated phosphorylation of UAP56 regulates the stability of UAP56. Our results will be helpful in further understanding mRNA metabolism, cell cycle progression, and the link between mRNA metabolism and cellular function.

Indexed as

Protein StabilityAnimalsCell Cycle ProteinsCell Line, TumorDEAD-box RNA HelicasesFlow CytometryHEK293 CellsHumansImmunoprecipitationMicePhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small InterferingTransfectionCell Cycle ProteinsDdx39b protein, mouseDEAD-box RNA HelicasesPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small Interfering

Identifiers

PMID21637952
OpenAlexW2022430107

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.