The RALF1-FERONIA interaction modulates endocytosis to mediate control of root growth in Arabidopsis

The RALF1-FERONIA interaction modulates endocytosis to mediate control of root growth in Arabidopsis. Yu, M., Li, R., Cui, Y., Chen, W., Li, B., Zhang, X., Bu, Y., Cao, Y., Xing, J., Jewaria, P. K., Li, X., Bhalerao, R. P., Yu, F., & Lin, J. Development, January, 2020.

Paper doi abstract bibtex

The interaction between the receptor-like kinase (RLK) FERONIA (FER) and the secreted peptide Rapid Alkalinization Factor 1 (RALF1) is vital for development and stress responses in Arabidopsis. Ligand-induced membrane dynamics affect the function of several RLKs, but the effects of the RALF1-FER interaction on the dynamics of FER and the ensuing effects on its functionality are poorly understood. Here, we show that RALF1 modulated the dynamics and partitioning of FER-GFP at the plasma membrane (PM). Moreover, FER was internalized by both clathrin-mediated endocytosis (CME) and clathrin-independent endocytosis (CIE) under steady state conditions. After RALF1 treatment, FER-GFP internalization was primarily enhanced via the CME pathway, raising FER-GFP levels in the vacuole. RALF1 treatment also modulated trafficking of other PM proteins such as PIN2-GFP and BRI1-GFP, increasing their vacuolar levels by enhancing their internalization. Importantly, blocking CME attenuated RALF1-mediated root growth inhibition independently of RALF1-induced early signaling, suggesting that the RALF1 can also exert its effects via the CME pathway. These findings reveal that the RALF1-FER interaction modulates plant growth and development and this may also involve endocytosis of PM proteins.

@article{yu_ralf1-feronia_2020,
	title = {The {RALF1}-{FERONIA} interaction modulates endocytosis to mediate control of root growth in \textit{{Arabidopsis}}},
	issn = {1477-9129, 0950-1991},
	url = {https://journals.biologists.com/dev/article/doi/10.1242/dev.189902/266898/The-RALF1-FERONIA-interaction-modulates},
	doi = {10.1242/dev.189902},
	abstract = {The interaction between the receptor-like kinase (RLK) FERONIA (FER) and the secreted peptide Rapid Alkalinization Factor 1 (RALF1) is vital for development and stress responses in Arabidopsis. Ligand-induced membrane dynamics affect the function of several RLKs, but the effects of the RALF1-FER interaction on the dynamics of FER and the ensuing effects on its functionality are poorly understood. Here, we show that RALF1 modulated the dynamics and partitioning of FER-GFP at the plasma membrane (PM). Moreover, FER was internalized by both clathrin-mediated endocytosis (CME) and clathrin-independent endocytosis (CIE) under steady state conditions. After RALF1 treatment, FER-GFP internalization was primarily enhanced via the CME pathway, raising FER-GFP levels in the vacuole. RALF1 treatment also modulated trafficking of other PM proteins such as PIN2-GFP and BRI1-GFP, increasing their vacuolar levels by enhancing their internalization. Importantly, blocking CME attenuated RALF1-mediated root growth inhibition independently of RALF1-induced early signaling, suggesting that the RALF1 can also exert its effects via the CME pathway. These findings reveal that the RALF1-FER interaction modulates plant growth and development and this may also involve endocytosis of PM proteins.},
	language = {en},
	urldate = {2021-06-07},
	journal = {Development},
	author = {Yu, Meng and Li, Ruili and Cui, Yaning and Chen, Weijun and Li, Bin and Zhang, Xi and Bu, Yufen and Cao, Yangyang and Xing, Jingjing and Jewaria, Pawan Kumar and Li, Xiaojuan and Bhalerao, Rishikesh P. and Yu, Feng and Lin, Jinxing},
	month = jan,
	year = {2020},
	pages = {dev.189902},
}

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Ligand-induced membrane dynamics affect the function of several RLKs, but the effects of the RALF1-FER interaction on the dynamics of FER and the ensuing effects on its functionality are poorly understood. Here, we show that RALF1 modulated the dynamics and partitioning of FER-GFP at the plasma membrane (PM). Moreover, FER was internalized by both clathrin-mediated endocytosis (CME) and clathrin-independent endocytosis (CIE) under steady state conditions. After RALF1 treatment, FER-GFP internalization was primarily enhanced via the CME pathway, raising FER-GFP levels in the vacuole. RALF1 treatment also modulated trafficking of other PM proteins such as PIN2-GFP and BRI1-GFP, increasing their vacuolar levels by enhancing their internalization. Importantly, blocking CME attenuated RALF1-mediated root growth inhibition independently of RALF1-induced early signaling, suggesting that the RALF1 can also exert its effects via the CME pathway. 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Ligand-induced membrane dynamics affect the function of several RLKs, but the effects of the RALF1-FER interaction on the dynamics of FER and the ensuing effects on its functionality are poorly understood. Here, we show that RALF1 modulated the dynamics and partitioning of FER-GFP at the plasma membrane (PM). Moreover, FER was internalized by both clathrin-mediated endocytosis (CME) and clathrin-independent endocytosis (CIE) under steady state conditions. After RALF1 treatment, FER-GFP internalization was primarily enhanced via the CME pathway, raising FER-GFP levels in the vacuole. RALF1 treatment also modulated trafficking of other PM proteins such as PIN2-GFP and BRI1-GFP, increasing their vacuolar levels by enhancing their internalization. Importantly, blocking CME attenuated RALF1-mediated root growth inhibition independently of RALF1-induced early signaling, suggesting that the RALF1 can also exert its effects via the CME pathway. 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