Summary
Autophagy is a highly selective cellular quality control pathway. Selective removal of autophagic cargo are mediated by cargo receptors that contain cargo binding domains and ATG8 interacting motifs to bridge the cargo with autophagosomes. Although cargo receptors are the key players linking autophagy to cellular quality control, most of them are still waiting to be uncovered in plants. Identification and characterization of novel cargo receptors will pave the way for future translational studies that aim to enhance stress tolerance in crop species.
The host lab recently identified an Endoplasmic reticulum (ER) autophagy receptor C53, that interacts with ATG8 via non-canonical shuffled ATG8 interacting motif. Besides, C53 is regulated by an enigmatic posttranslational modification called ufmylation through binding to another ubiquitin-like protein UFM1. Interestingly, ATG8-UFM1 interaction is mutually exclusive. However, the structural basis of C53-ATG8 or C53-UFM1 interaction are currently unknown. Also, the physiological roles of ufmylation and the ufmylated protein substrates have not been studied in plants.
In this proposal, I aim to structurally and genetically characterize C53-ATG8 and C53-UFM1 interaction. In parallel, using proteomics, I will determine the ufmylome, i.e., ufmylated protein catalogue in plants for the first time. Finally, I will move beyond model species Arabidopsis and establish autophagy and ufmylation studies in rice. Altogether, my studies will further our understanding of a novel ER quality control pathway in model plant species and beyond.
I will work at the Gregor Mendel Institute (GMI), Vienna BioCenter (VBC) in the lab of Yasin Dagdas. VBC is one of the largest life sciences hubs in Europe. It has a dynamic postdoc community, with structured training programs to prepare postdocs for independent careers. The cutting-edge research concepts, resources, and soft-skill training that I will gain will help me to establish my own lab.
The host lab recently identified an Endoplasmic reticulum (ER) autophagy receptor C53, that interacts with ATG8 via non-canonical shuffled ATG8 interacting motif. Besides, C53 is regulated by an enigmatic posttranslational modification called ufmylation through binding to another ubiquitin-like protein UFM1. Interestingly, ATG8-UFM1 interaction is mutually exclusive. However, the structural basis of C53-ATG8 or C53-UFM1 interaction are currently unknown. Also, the physiological roles of ufmylation and the ufmylated protein substrates have not been studied in plants.
In this proposal, I aim to structurally and genetically characterize C53-ATG8 and C53-UFM1 interaction. In parallel, using proteomics, I will determine the ufmylome, i.e., ufmylated protein catalogue in plants for the first time. Finally, I will move beyond model species Arabidopsis and establish autophagy and ufmylation studies in rice. Altogether, my studies will further our understanding of a novel ER quality control pathway in model plant species and beyond.
I will work at the Gregor Mendel Institute (GMI), Vienna BioCenter (VBC) in the lab of Yasin Dagdas. VBC is one of the largest life sciences hubs in Europe. It has a dynamic postdoc community, with structured training programs to prepare postdocs for independent careers. The cutting-edge research concepts, resources, and soft-skill training that I will gain will help me to establish my own lab.
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| Web resources: | https://cordis.europa.eu/project/id/101028611 |
| Start date: | 01-05-2021 |
| End date: | 30-04-2023 |
| Total budget - Public funding: | 186 167,04 Euro - 186 167,00 Euro |
Cordis data
Original description
Autophagy is a highly selective cellular quality control pathway. Selective removal of autophagic cargo are mediated by cargo receptors that contain cargo binding domains and ATG8 interacting motifs to bridge the cargo with autophagosomes. Although cargo receptors are the key players linking autophagy to cellular quality control, most of them are still waiting to be uncovered in plants. Identification and characterization of novel cargo receptors will pave the way for future translational studies that aim to enhance stress tolerance in crop species.The host lab recently identified an Endoplasmic reticulum (ER) autophagy receptor C53, that interacts with ATG8 via non-canonical shuffled ATG8 interacting motif. Besides, C53 is regulated by an enigmatic posttranslational modification called ufmylation through binding to another ubiquitin-like protein UFM1. Interestingly, ATG8-UFM1 interaction is mutually exclusive. However, the structural basis of C53-ATG8 or C53-UFM1 interaction are currently unknown. Also, the physiological roles of ufmylation and the ufmylated protein substrates have not been studied in plants.
In this proposal, I aim to structurally and genetically characterize C53-ATG8 and C53-UFM1 interaction. In parallel, using proteomics, I will determine the ufmylome, i.e., ufmylated protein catalogue in plants for the first time. Finally, I will move beyond model species Arabidopsis and establish autophagy and ufmylation studies in rice. Altogether, my studies will further our understanding of a novel ER quality control pathway in model plant species and beyond.
I will work at the Gregor Mendel Institute (GMI), Vienna BioCenter (VBC) in the lab of Yasin Dagdas. VBC is one of the largest life sciences hubs in Europe. It has a dynamic postdoc community, with structured training programs to prepare postdocs for independent careers. The cutting-edge research concepts, resources, and soft-skill training that I will gain will help me to establish my own lab.
Status
CLOSEDCall topic
MSCA-IF-2020Update Date
28-04-2024
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