Evidence map›Paper›PMID 27552928›Full record

ArticleScientific reports2016

Tyrosine phosphorylation and protein degradation control the transcriptional activity of WRKY involved in benzylisoquinoline alkaloid biosynthesis.

Yasuyuki Yamada, Fumihiko Sato

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

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  14. Genome-Wide Profiling ofFrontiers in plant science · 2021
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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

2 authors.

Yasuyuki YamadaDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.
Fumihiko SatoDivision of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Benzylisoquinoline alkaloids (BIQ) are among the most structurally diverse and pharmaceutically valuable secondary metabolites. A plant-specific WRKY-type transcription factor, CjWRKY1, was isolated from Coptis japonica and identified as a transcriptional activator of BIQ biosynthesis. However, the expression of CjWRKY1 gene alone was not sufficient for the activation of genes encoding biosynthetic enzymes. Here, we report the importance of post-translational regulation of CjWRKY1 in BIQ biosynthesis. First, we detected the differential accumulation of CjWRKY1 protein in two cell lines with similar CjWRKY1 gene expression but different levels of accumulated alkaloids. Further investigation of the WRKY protein identified the phosphorylation of the WRKYGQK core domain at Y115. The CjWRKY(Y115E) phosphorylation-mimic mutant showed loss of nuclear localization, DNA-binding activity, and transactivation activity compared to wild-type CjWRKY1. Rapid degradation of the CjWRKY1 protein was also confirmed following treatment with inhibitors of the 26S proteasome and protease inhibitors. The existence of two independent degradation pathways as well as protein phosphorylation suggests the fine-tuning of CjWRKY1 activities is involved in the regulation of biosynthesis of BIQs.

Indexed as

AlkaloidsBenzylisoquinolinesCell NucleusCells, CulturedCoptisDNAElectrophoretic Mobility Shift AssayGene Expression Regulation, PlantImmunoprecipitationLeupeptinsMutagenesis, Site-DirectedPhosphorylationPlant CellsPlant ProteinsProtease InhibitorsProteasome Endopeptidase ComplexAlkaloidsATP dependent 26S proteaseBenzylisoquinolinesbenzyloxycarbonylleucyl-leucyl-leucine aldehydeDNALeupeptinsPlant ProteinsProtease InhibitorsProteasome Endopeptidase ComplexTranscription FactorsTyrosine

Identifiers

PMID27552928
PMCPMC4995487

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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.