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Updated: Apr 11, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Precise protein post-translational modifications modulate ABI5 activity
Feifei Yu1, Yaorong Wu2, Qi Xie1
1State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, No.1 West Beichen Road, Chaoyang District, Beijing 100101, PR China; University of Chinese Academy of Sciences, Beijing 100049, PR China.
Post-translational modifications (PTMs) like phosphorylation, ubiquitination, and sumoylation precisely regulate abscisic acid-insensitive 5 (ABI5) stability and activity. This review highlights these PTMs, offering a model for studying plant hormone signaling regulators.
Area of Science:
- Plant Biology
- Molecular Biology
- Biochemistry
Background:
- Abscisic acid-insensitive 5 (ABI5) is a crucial transcription factor in abscisic acid (ABA) signaling.
- ABI5 regulates key plant processes including seed dormancy, germination, growth, and flowering time.
Purpose of the Study:
- To review the post-translational modifications (PTMs) that regulate ABI5.
- To highlight the interplay of phosphorylation, ubiquitination, and sumoylation in controlling ABI5 signaling.
Main Methods:
- Literature review of studies on ABI5 and its PTMs.
- Analysis of interactions between different PTMs affecting ABI5.
Main Results:
- Multiple PTMs, including phosphorylation, ubiquitination, and sumoylation, converge to control ABI5 stability and activity.
- These modifications act in concert to fine-tune ABI5-mediated ABA signaling.
Conclusions:
- ABI5 is a central node for PTMs within the ABA signaling pathway.
- This review provides a framework for investigating PTMs in other plant hormone signaling pathways.
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