Evidence map›Paper›PMID 28205154›Full record

ArticleRice (New York, N.Y.)2017

The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae.

Mingzhi Tang, Yuese Ning, Xiaoli Shu, Bo Dong, Hongyan Zhang, Dianxing Wu, Hua Wang, Guo-Liang Wang, Bo Zhou

Open access · goldAbstract read
In one paragraph

Article in Rice (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
30.4field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 94 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

9 authors at 5 institutions in 3 countries.

Mingzhi TangInstitute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.
Yuese NingInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Xiaoli ShuInstitute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.
Bo DongInstitute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Hongyan ZhangInstitute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Dianxing WuInstitute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.
Hua WangInstitute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Guo-Liang WangInstitute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Bo ZhouInstitute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China. b.zhou@irri.org.
ZheJiang Academy of Agricultural Sciences · CNZhejiang University · CNChinese Academy of Agricultural Sciences · CNInstitute of Plant Protection · CNInternational Rice Research Institute · PH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe effector AvrPiz-t of Magnaporthe oryzae has virulence function in rice. However, the mechanism underlying its virulence in host is not fully understood.

resultsIn this study, we analyzed the function of AvrPiz-t interacting protein 12 (APIP12) in rice immunity. APIP12 significantly bound to AvrPiz-t and APIP6 in its middle portion and N-terminus, respectively, in yeast two-hybrid assay. Glutathione S-transferase (GST) pull-down assay further verified the interactions of APIP12 with AvrPiz-t and APIP6. APIP12 encodes a homologue of nucleoporin protein Nup98 without the conserved domain of Phe-Gly repeats and has no orthologue in other plants. Both knockout and knockdown of APIP12 caused enhanced susceptibility of rice plants to virulent isolates of M. oryzae. The expression of some pathogenesis-related (PR) genes was reduced in both knockout and knockdown mutants, suggesting that APIP12 is required for the accumulation of transcripts of PR genes upon the infection. It is worth noting that neither knockout/knockdown nor overexpression of APIP12 attenuates Piz-t resistance.

conclusionsTaken together, our results demonstrate that APIP12 is a virulence target of AvrPiz-t and is involved in the basal resistance against M. oryzae in rice.

Indexed as

APIP12AvrPiz-tBlast resistanceNup98Protein-protein interaction

Identifiers

PMID28205154
PMCPMC5311014
OpenAlexW2588904408

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.