Evidence map›Paper›PMID 27031246›Full record

ArticlePLoS pathogens2016

The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice.

Chan Ho Park, Gautam Shirsekar, Maria Bellizzi, Songbiao Chen, Pattavipha Songkumarn, Xin Xie, Xuetao Shi, Yuese Ning, Bo Zhou, Pavinee Suttiviriya and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
26.7field-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

79 citing papers in PubMed, 200 citations in OpenAlex.

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  17. Proteolysis in plant immunity.The Plant cell · 2024
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  20. OsCAMTA3 Negatively Regulates Disease Resistance toInternational journal of molecular sciences · 2024
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19 more citing papers are in PubMed but not listed here.

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

13 authors at 4 institutions in 2 countries.

Chan Ho ParkDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Gautam ShirsekarDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Maria BellizziDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Songbiao ChenDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Pattavipha SongkumarnDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Xin XieState Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Xuetao ShiState Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Yuese NingState Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
Bo ZhouDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Pavinee SuttiviriyaDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Mo WangDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
Kenji UmemuraMeiji Seika Kaisha Ltd, Health & Bioscience Laboratories, Tokyo, Japan.
Guo-Liang WangDepartment of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
The Ohio State University · USChinese Academy of Agricultural Sciences · CNFujian Academy of Agricultural Sciences · CNInstitute of Plant Protection · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although nucleotide-binding domain, leucine-rich repeat (NLR) proteins are the major immune receptors in plants, the mechanism that controls their activation and immune signaling remains elusive. Here, we report that the avirulence effector AvrPiz-t from Magnaporthe oryzae targets the rice E3 ligase APIP10 for degradation, but that APIP10, in return, ubiquitinates AvrPiz-t and thereby causes its degradation. Silencing of APIP10 in the non-Piz-t background compromises the basal defense against M. oryzae. Conversely, silencing of APIP10 in the Piz-t background causes cell death, significant accumulation of Piz-t, and enhanced resistance to M. oryzae, suggesting that APIP10 is a negative regulator of Piz-t. We show that APIP10 promotes degradation of Piz-t via the 26S proteasome system. Furthermore, we demonstrate that AvrPiz-t stabilizes Piz-t during M. oryzae infection. Together, our results show that APIP10 is a novel E3 ligase that functionally connects the fungal effector AvrPiz-t to its NLR receptor Piz-t in rice.

Indexed as

MagnaportheOryzaPlant DiseasesUbiquitinationUbiquitin-Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID27031246
PMCPMC4816579
OpenAlexW2306516213

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.