Evidence map›Paper›PMID 25480368›Full record

ArticleThe Plant cell2014

Site-specific N-glycosylation of the S-locus receptor kinase and its role in the self-incompatibility response of the brassicaceae.

Masaya Yamamoto, Titima Tantikanjana, Takeshi Nishio, Mikhail E Nasrallah, June B Nasrallah

Abstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

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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

5 authors.

Masaya YamamotoSection of Plant Biology, School of Integrative Plant Science, Cornell University, Ithaca, New York 14850.
Titima TantikanjanaSection of Plant Biology, School of Integrative Plant Science, Cornell University, Ithaca, New York 14850.
Takeshi NishioGraduate School of Agricultural Science, Tohoku University, Sendai, Miyagi 981-855, Japan.
Mikhail E NasrallahSection of Plant Biology, School of Integrative Plant Science, Cornell University, Ithaca, New York 14850.
June B NasrallahSection of Plant Biology, School of Integrative Plant Science, Cornell University, Ithaca, New York 14850 jbn2@cornell.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The S-locus receptor kinase SRK is a highly polymorphic transmembrane kinase of the stigma epidermis. Through allele-specific interaction with its pollen coat-localized ligand, the S-locus cysteine-rich protein SCR, SRK is responsible for recognition and inhibition of self pollen in the self-incompatibility response of the Brassicaceae. The SRK extracellular ligand binding domain contains several potential N-glycosylation sites that exhibit varying degrees of conservation among SRK variants. However, the glycosylation status and functional importance of these sites are currently unclear. We investigated this issue in transgenic Arabidopsis thaliana stigmas that express the Arabidopsis lyrata SRKb variant and exhibit an incompatible response toward SCRb-expressing pollen. Analysis of single- and multiple-glycosylation site mutations of SRKb demonstrated that, although five of six potential N-glycosylation sites in SRKb are glycosylated in stigmas, N-glycosylation is not important for SCRb-dependent activation of SRKb. Rather, N-glycosylation functions primarily to ensure the proper and efficient subcellular trafficking of SRK to the plasma membrane. The study provides insight into the function of a receptor that regulates a critical phase of the plant life cycle and represents a valuable addition to the limited information available on the contribution of N-glycosylation to the subcellular trafficking and function of plant receptor kinases.

Indexed as

Amino Acid MotifsArabidopsisCell MembraneGlycosylationPlant ProteinsPlants, Genetically ModifiedPollenProtein KinasesSelf-Incompatibility in Flowering PlantsPlant ProteinsProtein KinasesS-receptor kinase

Identifiers

PMID25480368
PMCPMC4311203

What OpenQuestion holds

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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.