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

P. Wang, R. Pleskot, J. Zang, J. Winkler, J. Wang, K. Yperman, T. Zhang, K. Wang, J. Gong, Y. Guan, C. Richardson, P. Duckney, M. Vandorpe, E. Mylle, J. Fiserova, D. Van Damme, PJ. Hussey,

. 2019 ; 10 (1) : 5132. [pub] 20191113

Language English Country Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc20005704

Grant support
P01 CA095616 NCI NIH HHS - United States

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.

References provided by Crossref.org

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$a The Arabidopsis EH proteins (AtEH1/Pan1 and AtEH2/Pan1) are components of the endocytic TPLATE complex (TPC) which is essential for endocytosis. Both proteins are homologues of the yeast ARP2/3 complex activator, Pan1p. Here, we show that these proteins are also involved in actin cytoskeleton regulated autophagy. Both AtEH/Pan1 proteins localise to the plasma membrane and autophagosomes. Upon induction of autophagy, AtEH/Pan1 proteins recruit TPC and AP-2 subunits, clathrin, actin and ARP2/3 proteins to autophagosomes. Increased expression of AtEH/Pan1 proteins boosts autophagosome formation, suggesting independent and redundant pathways for actin-mediated autophagy in plants. Moreover, AtEHs/Pan1-regulated autophagosomes associate with ER-PM contact sites (EPCS) where AtEH1/Pan1 interacts with VAP27-1. Knock-down expression of either AtEH1/Pan1 or VAP27-1 makes plants more susceptible to nutrient depleted conditions, indicating that the autophagy pathway is perturbed. In conclusion, we identify the existence of an autophagy-dependent pathway in plants to degrade endocytic components, starting at the EPCS through the interaction among AtEH/Pan1, actin cytoskeleton and the EPCS resident protein VAP27-1.
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$a Pleskot, Roman $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium.
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$a Zang, Jingze $u Department of Biosciences, Durham University, South road, Durham, DH1 3LE, UK. Key Laboratory of Horticultural Plant Biology (MOE), College of Horticulture and Forestry Sciences, Huazhong Agricultural University, Wuhan, 430070, Hubei Province, PR China.
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$a Winkler, Joanna $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium.
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$a Wang, Jie $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium.
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$a Yperman, Klaas $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium.
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$a Zhang, Tong $u Key Laboratory of Horticultural Plant Biology (MOE), College of Horticulture and Forestry Sciences, Huazhong Agricultural University, Wuhan, 430070, Hubei Province, PR China.
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$a Wang, Kun $u Key Laboratory of Horticultural Plant Biology (MOE), College of Horticulture and Forestry Sciences, Huazhong Agricultural University, Wuhan, 430070, Hubei Province, PR China.
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$a Guan, Yajie $u Key Laboratory of Horticultural Plant Biology (MOE), College of Horticulture and Forestry Sciences, Huazhong Agricultural University, Wuhan, 430070, Hubei Province, PR China.
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$a Richardson, Christine $u Department of Biosciences, Durham University, South road, Durham, DH1 3LE, UK.
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$a Duckney, Patrick $u Department of Biosciences, Durham University, South road, Durham, DH1 3LE, UK.
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$a Vandorpe, Michael $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium.
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$a Mylle, Evelien $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium.
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$a Fiserova, Jindriska $u Department of Biosciences, Durham University, South road, Durham, DH1 3LE, UK. Department of Biology of the Cell Nucleus, Institute of Molecular Genetics CAS, v.v.i., Vídeňská 1083, Prague, 14200, Czech Republic.
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$a Van Damme, Daniel $u Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 71, 9052, Ghent, Belgium. dadam@psb.vib-ugent.be. VIB Center for Plant Systems Biology, Technologiepark 71, 9052, Ghent, Belgium. dadam@psb.vib-ugent.be.
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