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Updated: Jun 10, 2026
10:07
Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Plant phosphopeptide-binding proteins as signaling mediators
Tufan Gökirmak1, Anna-Lisa Paul, Robert J Ferl
1Program in Plant Molecular and Cellular Biology, Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611-0690, USA.
Current Opinion in Plant Biology
|July 20, 2010
Summary
Plant 14-3-3 proteins regulate cellular signaling by binding to phosphorylated proteins. These interactions are vital for cellular processes and signal transduction pathways in plants.
Area of Science:
- Plant molecular biology
- Cellular signaling
- Protein-protein interactions
Background:
- Protein phosphorylation is a key regulator of cellular processes, including signaling.
- Phosphorylation-dependent protein interactions are critical for this regulation.
- In plants, 14-3-3 proteins are major phosphopeptide-binding proteins, alongside FHA domain proteins.
Purpose of the Study:
- To highlight the crucial role of 14-3-3 proteins in plant cellular regulation.
- To emphasize the expanding understanding of 14-3-3 proteins in plant signal transduction.
Main Methods:
- Literature review of existing studies on plant 14-3-3 proteins.
- Analysis of reported interactions between 14-3-3 proteins and their phosphorylated targets.
- Synthesis of findings regarding 14-3-3 involvement in metabolic enzymes and signaling pathways.
Main Results:
- 14-3-3 proteins interact with diverse phosphorylated target proteins across eukaryotes.
- Initially associated with metabolic enzyme regulation, plant 14-3-3s are increasingly recognized for their roles in signal transduction.
- Plant 14-3-3 proteins interact with key components of signaling pathways.
Conclusions:
- Plant 14-3-3 proteins are essential regulators of cellular processes through interactions with phosphorylated targets.
- The role of 14-3-3 proteins in plant signaling pathways is a significant and growing area of research.
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