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Correlation of Autophagosome Formation with Degradation and Endocytosis Arabidopsis Regulator of G-Protein Signaling (RGS1) through ATG8a
Y. Jiao, M. Srba, J. Wang, W. Chen,
Language English Country Switzerland
Document type Journal Article
Grant support
R01 GM065989
NIGMS NIH HHS - United States
31170250
National Natural Science Foundation of China
31570256
National Natural Science Foundation of China
NLK
Free Medical Journals
from 2000
Freely Accessible Science Journals
from 2000
PubMed Central
from 2007
Europe PubMed Central
from 2007
ProQuest Central
from 2000-03-01
Open Access Digital Library
from 2000-01-01
Open Access Digital Library
from 2007-01-01
Health & Medicine (ProQuest)
from 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
from 2000
PubMed
31461856
DOI
10.3390/ijms20174190
Knihovny.cz E-resources
- MeSH
- Arabidopsis MeSH
- Autophagy MeSH
- Autophagosomes metabolism MeSH
- Endocytosis MeSH
- Arabidopsis Proteins genetics metabolism MeSH
- RGS Proteins genetics metabolism MeSH
- Proteolysis MeSH
- Autophagy-Related Protein 8 Family genetics metabolism MeSH
- Signal Transduction MeSH
- Publication type
- Journal Article MeSH
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.
References provided by Crossref.org
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