Plant AtEH/Pan1 proteins drive autophagosome formation at ER-PM contact sites with actin and endocytic machinery

Wang, Pengwei; Pleskot, Roman; Zang, Jingze; Winkler, Joanna; Wang, Jie; Yperman, Klaas; Zhang, Tong; Wang, Kun; Gong, Jinli; Guan, Yajie; Richardson, Christine; Duckney, Patrick; Vandorpe, Michael; Mylle, Evelien; Fiserova, Jindriska; Van Damme, Daniel; Hussey, Patrick J.

Abstract

The Arabidopsis EH proteins (AtEH1/Pan1 and AtEH2/Pan1) are components of the endocytic TPLATE complex (TPC) which is essential for endocytosis. Both proteins are homologues of the yeast ARP2/3 complex activator, Pan1p. Here, we show that these proteins are also involved in actin cytoskeleton regulated autophagy. Both AtEH/Pan1 proteins localise to the plasma membrane and autophagosomes. Upon induction of autophagy, AtEH/Pan1 proteins recruit TPC and AP-2 subunits, clathrin, actin and ARP2/3 proteins to autophagosomes. Increased expression of AtEH/Pan1 proteins boosts autophagosome formation, suggesting independent and redundant pathways for actin-mediated autophagy in plants. Moreover, AtEHs/Pan1-regulated autophagosomes associate with ER-PM contact sites (EPCS) where AtEH1/Pan1 interacts with VAP27-1. Knock-down expression of either AtEH1/Pan1 or VAP27-1 makes plants more susceptible to nutrient depleted conditions, indicating that the autophagy pathway is perturbed. In conclusion, we identify the existence of an autophagy-dependent pathway in plants to degrade endocytic components, starting at the EPCS through the interaction among AtEH/Pan1, actin cytoskeleton and the EPCS resident protein VAP27-1.

Citation

Wang, P., Pleskot, R., Zang, J., Winkler, J., Wang, J., Yperman, K., Zhang, T., Wang, K., Gong, J., Guan, Y., Richardson, C., Duckney, P., Vandorpe, M., Mylle, E., Fiserova, J., Van Damme, D., & Hussey, P. J. (2019). Plant AtEH/Pan1 proteins drive autophagosome formation at ER-PM contact sites with actin and endocytic machinery. Nature Communications, 10(1), Article 5132. https://doi.org/10.1038/s41467-019-12782-6

• Journal Article Type: Article
• Acceptance Date: Sep 25, 2019
• Online Publication Date: Nov 13, 2019
• Publication Date: Nov 13, 2019
• Deposit Date: Nov 15, 2019
• Publicly Available Date: Nov 15, 2019
• Journal: Nature Communications
• Publisher: Nature Research
• Peer Reviewed: Peer Reviewed
• Volume: 10
• Issue: 1
• Article Number: 5132
• DOI: https://doi.org/10.1038/s41467-019-12782-6
• Public URL: https://durham-repository.worktribe.com/output/1313848