Evidence map›Paper›PMID 35218353›Full record

ArticlePlant physiology2022

GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif.

Octavina C A Sukarta, Qi Zheng, Erik J Slootweg, Mark Mekken, Melanie Mendel, Vera Putker, André Bertran, Anouk Brand, Hein Overmars, Rikus Pomp and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2022. 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
2.7field-weighted citation impact, top 11% 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, 14 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

14 authors at 1 institution in 1 country.

Octavina C A SukartaLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0003-0520-2392
Qi ZhengLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.
Erik J SlootwegLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0001-9935-7728
Mark MekkenLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.
Melanie MendelLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0003-2409-7479
Vera PutkerLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.
André BertranLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0002-8993-4357
Anouk BrandLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0002-2346-2641
Hein OvermarsLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0003-2461-4026
Rikus PompLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.
Jan RoosienLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.
Sjef BoerenLaboratory of Biochemistry, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0002-0847-8821
Geert SmantLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0001-6094-8686
Aska GoverseLaboratory of Nematology, Wageningen University & Research, Wageningen, The Netherlands.ORCID 0000-0002-7399-8743
Wageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of intracellular plant nucleotide-binding leucine-rich repeat (NB-LRR) immune receptors is fine-tuned by interactions between the receptors and their partners. Identifying NB-LRR interacting proteins is therefore crucial to advance our understanding of how these receptors function. A co-immunoprecipitation/mass spectrometry screening was performed in Nicotiana benthamiana to identify host proteins associated with the resistance protein Gpa2, a CC-NB-LRR immune receptor conferring resistance against the potato cyst nematode Globodera pallida. A combination of biochemical, cellular, and functional assays was used to assess the role of a candidate interactor in defense. A N. benthamiana homolog of the GLYCINE-RICH RNA-BINDING PROTEIN7 (NbGRP7) protein was prioritized as a Gpa2-interacting protein for further investigations. NbGRP7 also associates in planta with the homologous Rx1 receptor, which confers immunity to Potato Virus X. We show that NbGRP7 positively regulates extreme resistance by Rx1 and cell death by Gpa2. Mutating the NbGRP7 RNA recognition motif (RRM) compromises its role in Rx1-mediated defense. Strikingly, ectopic NbGRP7 expression is likely to impact the steady-state levels of Rx1, which relies on an intact RRM. Our findings illustrate that NbGRP7 is a pro-immune component in effector-triggered immunity by regulating Gpa2/Rx1 function at a posttranscriptional level.

Indexed as

Plant ProteinsTylenchoideaAnimalsGlycinePlant DiseasesPlant ImmunityReceptors, ImmunologicRNA-Binding ProteinsRNA Recognition MotifGlycinePlant ProteinsReceptors, ImmunologicRNA-Binding Proteins

Identifiers

PMID35218353
PMCPMC9157115
OpenAlexW4214725676

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.