Evidence map›Paper›PMID 26244501›Full record

ArticlePloS one2015

Avian Reovirus Protein p17 Functions as a Nucleoporin Tpr Suppressor Leading to Activation of p53, p21 and PTEN and Inactivation of PI3K/AKT/mTOR and ERK Signaling Pathways.

Wei-Ru Huang, Hung-Chuan Chiu, Tsai-Ling Liao, Kuo-Pin Chuang, Wing-Ling Shih, Hung-Jen Liu

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 45 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Wei-Ru HuangInstitute of Molecular Biology, National Chung Hsing University, Taichung, 402, Taiwan.
Hung-Chuan ChiuInstitute of Molecular Biology, National Chung Hsing University, Taichung, 402, Taiwan.
Tsai-Ling LiaoDepartment of Medical Research, Taichung Veterans General Hospital, Taichung, 402, Taiwan.
Kuo-Pin ChuangGraduate Institute of Animal Vaccine Technology, National Pingtung University of Science and Technology, Pingtung, 912, Taiwan.
Wing-Ling ShihDepartment of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung, 912, Taiwan.
Hung-Jen LiuInstitute of Molecular Biology, National Chung Hsing University, Taichung, 402, Taiwan; Agricultural Biotechnology Center, National Chung Hsing University, Taichung, 402, Taiwan; Rong Hsing Research Center for Translational Medicine, National Chung Hsing University, Taichung, 402, Taiwan.
National Chung Hsing University · TWNational Pingtung University of Science and Technology · TWTaichung Veterans General Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Avian reovirus (ARV) protein p17 has been shown to regulate cell cycle and autophagy by activation of p53/PTEN pathway; nevertheless, it is still unclear how p53 and PTEN are activated by p17. Here, we report for the first time that p17 functions as a nucleoporin Tpr suppressor that leads to p53 nuclear accumulation and consequently activates p53, p21, and PTEN. The nuclear localization signal (119IAAKRGRQLD128) of p17 has been identified for Tpr binding. This study has shown that Tpr suppression occurs by p17 interacting with Tpr and by reducing the transcription level of Tpr, which together inhibit Tpr function. In addition to upregulation of PTEN by activation of p53 pathway, this study also suggests that ARV protein p17 acts as a positive regulator of PTEN. ARV p17 stabilizes PTEN by stimulating phosphorylation of cytoplasmic PTEN and by elevating Rak-PTEN association to prevent it from E3 ligase NEDD4-1 targeting. To activate PTEN, p17 is able to promote β-arrestin-mediated PTEN translocation from the cytoplasm to the plasma membrane via a Rock-1-dependent manner. The accumulation of p53 in the nucleus induces the PTEN- and p21-mediated downregulation of cyclin D1 and CDK4. Furthermore, Tpr and CDK4 knockdown increased virus production in contrast to depletion of p53, PTEN, and LC3 reducing virus yield. Taken together, our data suggest that p17-mediated Tpr suppression positively regulates p53, PTEN, and p21 and negatively regulates PI3K/AKT/mTOR and ERK signaling pathways, both of which are beneficial for virus replication.

Indexed as

Host-Pathogen InteractionsSignal TransductionAmino Acid SequenceAnimalsCell LineChlorocebus aethiopsHumansMAP Kinase Signaling SystemNuclear Localization SignalsNuclear Pore Complex ProteinsOrthoreovirus, AvianPhosphatidylinositol 3-KinasesProtein Interaction MapsProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseReoviridae InfectionsNuclear Localization SignalsNuclear Pore Complex ProteinsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseTOR Serine-Threonine KinasesTumor Suppressor Protein p53Viral Proteins

Identifiers

PMID26244501
PMCPMC4526660
OpenAlexW4229633290

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.