Phosphorylation Alters the Interaction of the Arabidopsis Phosphotransfer Protein AHP1 with Its Sensor Kinase ETR1
2011
Phosphorylation Affects Interaction of ETR1 and AHP1 in Ethylene Signaling
publication
Evidence: moderate
Author Information
Author(s): Benjamin Scharein, Georg Groth
Primary Institution: Biochemical Plant Physiology, Heinrich-Heine Universität, Düsseldorf, Germany
Hypothesis
How does the phosphorylation status of ETR1 and AHP1 affect their interaction in ethylene signaling?
Conclusion
Phosphorylation significantly influences the interaction between ETR1 and AHP1, with tight binding occurring when one is phosphorylated and the other is not.
Supporting Evidence
- Phosphorylation reduces the affinity of ETR1 for AHP1 when both are in their phosphorylated or non-phosphorylated forms.
- Binding of ethylene or its agonists decreases the interaction between ETR1 and AHP1.
- Fluorescence polarization assays provided quantitative insights into the stability of the ETR1-AHP1 complex.
Takeaway
This study shows that when one protein is 'turned on' by phosphorylation, it can better connect with another protein, helping plants respond to a hormone called ethylene.
Methodology
Fluorescence polarization was used to analyze the interaction between ETR1 and AHP1 under different phosphorylation states.
Digital Object Identifier (DOI)
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