Maxim Faroux (Kiel University)
FRET analyses showed that the aquaporin PIP2;1 (violet) is in spatial proximity to the phytosulfokine receptor PSKR1 (red) in the plasma membrane. The kinase domain (KD) of PSKR1 phosphorylates cytosolic fragments of PIP2;1 in vitro. Graph: Maxim Faroux (CAU Kiel)
Maxim Faroux's Master thesis was awarded with the Prize for the Best Plant Science Master Thesis, which was carried out at Kiel University in the year 2021
Title: The aquaporin PIP2;1 as a potential interaction partner of PSKR1
The aquaporin PIP2;1 exists in close proximity to PSKR1 in the plasma membrane and might be a kinase substrate of PSKR1
The peptide hormone phytosulfokine (PSK) is perceived by the membrane-bound LRR-receptor kinases PSKR1 and PSKR2 in Arabidopsis thaliana. Plants lacking both receptors are smaller. Three types of Förster resonance energy transfer (FRET) analyses were established to study proximity between PSKR1 and PIP2;1: FRET sensitized emission (FRET SE), using both confocal laser scanning microscopy and a plate reader, and FRET acceptor photobleaching (FRET AB). Data from FRET AB indicated spatial proximity between PIP2;1 and PSKR1 and phosphorylation of PIP2;1 by the kinase domain of PSKR1 was shown in vitro. Phosphosite mapping and functional analysis of the PIP2;1 phosphosites will provide insight into PIP2;1 regulation by PSKR1.
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Maxim Faroux conducted this work at the botanical institute in the group of Prof. Dr. Margret Sauter.