Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 17, Pages -Publisher
MDPI
DOI: 10.3390/ijms20174190
Keywords
Arabidopsis; regulator of G signaling protein 1; autophagy; nutrient starvation; glucose; BY-2
Funding
- National Natural Science Foundation of China [31570256, 31170250]
- Natural Science Foundation of Guangdong Province, China [2014A030313420]
- science and technology project of Guangzhou [201805010002, R01GM065989]
- NSF [MCB-0718202]
- Ministry of Education, Youth and Sports of the Czech Republic [NPUI LO1417, LD15149, RGS11-283-GFP, RGS11-413-GFP, RGS11-283,414-459, RGS11-250-GFP, RGS114-250-GFP]
- UNC-Chapel Hill School of Medicine of USA
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Damaged or unwanted cellular proteins are degraded by either autophagy or the ubiquitin/proteasome pathway. In Arabidopsis thaliana, sensing of D-glucose is achieved by the heterotrimeric G protein complex and regulator of G-protein signaling 1 (AtRGS1). Here, we showed that starvation increases proteasome-independent AtRGS1 degradation, and it is correlated with increased autophagic flux. RGS1 promoted the production of autophagosomes and autophagic flux; RGS1-yellow fluorescent protein (YFP) was surrounded by vacuolar dye FM4-64 (red fluorescence). RGS1 and autophagosomes co-localized in the root cells of Arabidopsis and BY-2 cells. We demonstrated that the autophagosome marker ATG8a interacts with AtRGS1 and its shorter form with truncation of the seven transmembrane and RGS1 domains in planta. Altogether, our data indicated the correlation of autophagosome formation with degradation and endocytosis of AtRGS1 through ATG8a.
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