Bridging the gap between selective autophagy and endoplasmic reticulum homeostasis
Yasin Dagdas is a Group Leader at the Gregor Mendel Institute since 2017. Prior to that, he was a postdoc at The Sainsbury Laboratory, UK. He did his PhD at University of Exeter, UK.
- Institute Gregor Mendel Institute of Plant Molecular Biology
- Phone +43 1 79044 9850
- Mail firstname.lastname@example.org
- Web https://www.gmi.oeaw.ac.at/research-groups/yasin-dagdas/
Projects within consortium
The endoplasmic reticulum (ER) mediates folding and maturation of ~40% of the cellular proteome. Eukaryotes have evolved sophisticated quality control mechanisms to ensure proteostasis in the ER. One of these pathways that mediate removal of certain domains of the ER via autophagy is called ER-phagy. In this project, we will try to understand how ER-phagy cross-talks with the other ER quality control pathways.
Disruption of Endoplasmic reticulum homeostasis leads to the activation of a highly conserved homeostatic mechanism, termed the Unfolded Protein Response (UPR). UPR involves increasing the protein folding capacity of the ER, as well as degrading terminally misfolded proteins. Degradation of misfolded proteins are carried out by two pathways: (i) ER-associated degradation (ERAD) pathway, which involves translocation of unfolded proteins from ER to cytosol, and degradation at the proteasome; (ii) selective autophagy – aka ER-phagy – that mediates degradation of a part of the ER, which presumably contains unfolded proteins. How and when the cell decides to channel unfolded proteins to one of these degradation pathways are currently unknown.
Recently, we identified a connection between autophagy and UPR in plants. During the course of this SFB project, in collaboration with Beli, Clausen, Karagoz, Kohler and Martens labs, we would like to (i) biophysically and structurally characterize the protein complexes that connect UPR to autophagy (ii) explore how the cell decides to employ selective autophagy or the ERAD pathway, and (iii) perform in vitro and in vivo reconstitution experiments to mechanistically understand the pathway in detail. By the completion of this project, we aim to develop a comprehensive understanding of the cross-talk between selective autophagy and ER quality control pathways, which could allow us to develop translational means to enhance ER stress tolerance and productivity.
Victor Sanchez de Medina
Targeted Protein Degradation related publications by Group Dagdas
- 2022 Characterization of ATG8-Family Interactors by Isothermal Titration Calorimetry Methods in Molecular Biology Go to publication →
- 2022 Plant autophagosomes mature into amphisomes prior to their delivery to the central vacuole Journal of Cell Biology Go to publication →
- 2022 Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and C53-mediated autophagy bioRxiv Go to publication →
- 2022 Autophagy promotes programmed cell death and corpse clearance in specific cell types of the Arabidopsis root cap Current Biology Go to publication →
- 2022 Molecular mechanisms of endomembrane trafficking in plants Plant Cell Go to publication →
- 2021 Proteasome and selective autophagy: Brothers-in-arms for organelle quality control Current Opinion in Plant Biology Go to publication →
- 2021 An oomycete effector subverts host vesicle trafficking to channel starvation-induced autophagy to the pathogen interface eLife Go to publication →
- 2020 EXO70D isoforms mediate selective autophagic degradation of type-A ARR proteins to regulate cytokinin sensitivity Proc. Natl. Acad. Sci. USA Go to publication →
- 2020 A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress eLife Go to publication →
- 2020 Autophagy mediates temporary reprogramming and dedifferentiation in plant somatic cells EMBO Journal Go to publication →
- 2019 N-terminal β-strand underpins biochemical specialization of an ATG8 isoform PLoS Biology Go to publication →
- 2018 Host autophagy machinery is diverted to the pathogen interface to mediate focal defense responses against the Irish potato famine pathogen eLife Go to publication →
- 2016 Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54 J. Biol. Chem. Go to publication →
- 2016 An effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor eLife Go to publication →