Abstract
WRINKLED1 (WRI1), a member of the APETALA2 (AP2) class of transcription factors, positively regulates glycolysis and lipid biosynthesis in Arabidopsis thaliana. Here, we identify mechanistic links between KIN10, the major SUCROSE NON-FERMENTATION1-RELATED KINASE1 involved in sugar/energy homeostasis, and the posttranslational regulation of WRI1. Transient expression of WRI1 with OLEOSIN1 in Nicotiana benthamiana stimulates triacylglycerol accumulation, but their coexpression with KIN10 abrogates this effect by inducing proteasomal degradation of WRI1. While WRI1 lacks canonical KIN10 target sequences, we demonstrated direct KIN10-dependent phosphorylation of WRI1 using purified Escherichia coli-expressed components. The resulting phosphorylated WRI1 was more rapidly degraded than native WRI1 in cell-free degradation assays. WRI1 phosphorylation was localized to two variants of the canonical KIN10 recognition sequence, one in each of its two AP2 DNA binding domains. Conversion of the phosphorylation sites at Thr-70 and Ser-166 to Ala resulted in a loss of KIN10-dependent phosphorylation, and when coexpressed with KIN10 the WRI1 double mutant accumulated to 2- to 3-fold higher levels than native WRI1. KIN10-dependent degradation of WRI1 provides a homeostatic mechanism that favors lipid biosynthesis when intracellular sugar levels are elevated and KIN10 is inhibited; conversely, glycolysis and lipid biosynthesis are curtailed as sugar levels decrease and KIN10 regains activity.
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Claims 7
Claim · model-written summary
WRI1 with OLEOSIN1 stimulated triacylglycerol accumulation in Nicotiana benthamiana.
- Taxon
- Nicotiana benthamiana
Nicotiana benthamianae0 - Treatment
- Transient expression of WRI1 with OLEOSIN1e0
- Gene
- WRI1 with OLEOSIN1e0
- Outcome
- triacylglycerol accumulatione0
- Direction
- stimulatese0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Transient expression of WRI1 with OLEOSIN1 in Nicotiana benthamiana stimulates triacylglycerol accumulation”
Claim · model-written summary
Coexpression with KIN10 abrogated triacylglycerol accumulation.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Treatment
- coexpression with KIN10e0
- Gene
- KIN10e0
- Outcome
- this effecte0
- Direction
- abrogatese0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“their coexpression with KIN10 abrogates this effect by inducing proteasomal degradation of WRI1”
t0“in Arabidopsis thaliana”
Claim · model-written summary
KIN10 directly phosphorylated WRI1.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Gene
- WRI1e0
- Outcome
- direct KIN10-dependent phosphorylation of WRI1e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“we demonstrated direct KIN10-dependent phosphorylation of WRI1 using purified Escherichia coli-expressed components”
t0“in Arabidopsis thaliana”
Claim · model-written summary
Phosphorylated WRI1 degraded faster than native WRI1.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Gene
- WRI1e0
- Outcome
- degradede0
- Direction
- more rapidlye0
- Comparator
- native WRI1e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“phosphorylated WRI1 was more rapidly degraded than native WRI1 in cell-free degradation assays”
t0“in Arabidopsis thaliana”
Claim · model-written summary
WRI1 phosphorylation localized to variants in its two AP2 DNA binding domains.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Gene
- WRI1e0
- Outcome
- phosphorylation was localized to two variants of the canonical KIN10 recognition sequencee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“WRI1 phosphorylation was localized to two variants of the canonical KIN10 recognition sequence, one in each of its two AP2 DNA binding domains”
t0“in Arabidopsis thaliana”
Claim · model-written summary
Ala conversion at Thr-70 and Ser-166 eliminated KIN10-dependent phosphorylation.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Treatment
- Conversion of the phosphorylation sites at Thr-70 and Ser-166 to Alae0
- Outcome
- KIN10-dependent phosphorylatione0
- Direction
- losse0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Conversion of the phosphorylation sites at Thr-70 and Ser-166 to Ala resulted in a loss of KIN10-dependent phosphorylation”
t0“in Arabidopsis thaliana”
Claim · model-written summary
The WRI1 double mutant accumulated at 2- to 3-fold higher levels than native WRI1 with KIN10.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Treatment
- coexpressed with KIN10e0
- Outcome
- WRI1 double mutant accumulatede0
- Direction
- highere0
- Value
- 2- to 3-folde0
- Comparator
- native WRI1e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“when coexpressed with KIN10 the WRI1 double mutant accumulated to 2- to 3-fold higher levels than native WRI1”
t0“in Arabidopsis thaliana”
The same questions in other papers
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