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Updated: Sep 9, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
Published on: March 14, 2021
Phosphorylation-regulated SEC14-GOLD PATELLIN lipid transfer proteins
Jannik Hornbergs1, Petra Bauer2
1Institute of Botany, Heinrich-Heine-University, 40225 Düsseldorf, Germany.
None:
The SEC14-GOLD family of phosphatidylinositol (PI) transfer proteins, known as PATELLIN (PATL) proteins in plants, are key regulators of plasma membrane (PM)-related signaling processes. They function through multifaceted interactions involving a SEC14 lipid-binding domain, GOLD domain, and their N-terminal region. Protein phosphorylation is crucial for modulating protein and phospholipid interactions, but phosphorylation of SEC14 proteins remains understudied. Phosphoproteomics data from Arabidopsis thaliana indicates two major phosphorylation hubs within the N-terminal and the conserved SEC14-GOLD regions in the PATLs. These phosphorylation patterns vary in response to environmental and hormonal stress-related factors. Understanding how PATL proteins are phosphorylated can offer insights into PATL-membrane interactions and their functional roles in cell physiology, providing new strategies for plant adaptation and stress resilience in crops.
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