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An Arabidopsis SUMO E3 Ligase, SIZ1, Negatively Regulates Photomorphogenesis by Promoting COP1 ActivitySugar signaling regulation by Arabidopsis SIZ1-driven sumoylation is independent of salicylic acid.Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response.The Kinase Activity of Calcineurin B-like Interacting Protein Kinase 26 (CIPK26) Influences Its Own Stability and that of the ABA-regulated Ubiquitin Ligase, Keep on Going (KEG).Protein sumoylation and phosphorylation intersect in Arabidopsis signaling.Plant SnRK1 Kinases: Structure, Regulation, and Function.The plant energy sensor: evolutionary conservation and divergence of SnRK1 structure, regulation, and function.Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase Is Phosphorylated during Seed Development.Arabidopsis TCP Transcription Factors Interact with the SUMO Conjugating Machinery in Nuclear Foci.Upstream kinases of plant SnRKs are involved in salt stress tolerance.Phosphorylation of WRINKLED1 by KIN10 Results in Its Proteasomal Degradation, Providing a Link between Energy Homeostasis and Lipid Biosynthesis.The Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stability.The Arabidopsis SUMO E3 ligase SIZ1 mediates the temperature dependent trade-off between plant immunity and growth.
P2860
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P2860
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2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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2015年学术文章
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name
SUMOylation represses SnRK1 signaling in Arabidopsis.
@en
SUMOylation represses SnRK1 signaling in Arabidopsis.
@nl
type
label
SUMOylation represses SnRK1 signaling in Arabidopsis.
@en
SUMOylation represses SnRK1 signaling in Arabidopsis.
@nl
altLabel
SUMOylation represses SnRK1 signaling in Arabidopsis
@en
prefLabel
SUMOylation represses SnRK1 signaling in Arabidopsis.
@en
SUMOylation represses SnRK1 signaling in Arabidopsis.
@nl
P2093
P2860
P50
P921
P356
P1433
P1476
SUMOylation represses SnRK1 signaling in Arabidopsis
@en
P2093
Ari Sadanandom
Konstantin Tomanov
Noémia Fernandes
Rafal Butowt
P2860
P304
P356
10.1111/TPJ.13096
P407
P50
P577
2016-01-01T00:00:00Z