Evidence map›Paper›PMID 25891985›Full record

ArticleMolecular plant pathology2016

SOBIR1 requires the GxxxG dimerization motif in its transmembrane domain to form constitutive complexes with receptor-like proteins.

Guozhi Bi, Thomas W H Liebrand, Ruby R Bye, Jelle Postma, Aranka M van der Burgh, Silke Robatzek, Xiangyang Xu, Matthieu H A J Joosten

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2016. 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
8.8field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 59 citations in OpenAlex.

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  9. Population studies of the wild tomato speciesProceedings. Biological sciences · 2020
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  10. Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
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  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Guozhi BiCollege of Horticulture, Northeast Agricultural University, Harbin, 150030, China.
Thomas W H LiebrandLaboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, the Netherlands.
Ruby R ByeLaboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, the Netherlands.
Jelle PostmaThe Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, UK.
Aranka M van der BurghLaboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, the Netherlands.
Silke RobatzekThe Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, UK.
Xiangyang XuCollege of Horticulture, Northeast Agricultural University, Harbin, 150030, China.
Matthieu H A J JoostenLaboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, the Netherlands.
Wageningen University & Research · NLNortheast Agricultural University · CNNorwich Research Park · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor-like proteins (RLPs), forming an important group of transmembrane receptors in plants, play roles in development and immunity. RLPs contain extracellular leucine-rich repeats (LRRs) and, in contrast with receptor-like kinases (RLKs), lack a cytoplasmic kinase required for the initiation of downstream signalling. Recent studies have revealed that the RLK SOBIR1/EVR (SUPPRESSOR OF BIR1-1/EVERSHED) specifically interacts with RLPs. SOBIR1 stabilizes RLPs and is required for their function. However, the mechanism by which SOBIR1 associates with RLPs and regulates RLP function remains unknown. The Cf immune receptors of tomato (Solanum lycopersicum), mediating resistance to the fungus Cladosporium fulvum, are RLPs that also interact with SOBIR1. Here, we show that both the LRR and kinase domain of SOBIR1 are dispensable for association with the RLP Cf-4, whereas the highly conserved GxxxGxxxG motif present in the transmembrane domain of SOBIR1 is essential for its interaction with Cf-4 and additional RLPs. Complementation assays in Nicotiana benthamiana, in which endogenous SOBIR1 levels were knocked down by virus-induced gene silencing, showed that the LRR domain as well as the kinase activity of SOBIR1 are required for the Cf-4/Avr4-triggered hypersensitive response (HR). In contrast, the LRRs and kinase activity of SOBIR1 are not required for facilitation of Cf-4 accumulation. Together, these results suggest that, in addition to being a stabilizing scaffold for RLPs, SOBIR1 is also required for the initiation of downstream signalling through its kinase domain.

Indexed as

Protein MultimerizationAmino Acid MotifsAmino Acid SequenceMolecular Sequence DataMultiprotein ComplexesNicotianaPhylogenyPlant ProteinsPlants, Genetically ModifiedProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidStructure-Activity RelationshipMultiprotein ComplexesPlant Proteinsdefence signallingdevelopmentplant immunityreceptor complexreceptor-like kinase (RLK)receptor-like protein (RLP)SOBIR1

Identifiers

PMID25891985
PMCPMC6638328
OpenAlexW2100467491

What OpenQuestion holds

Textmetadata
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.