Exocyst subunit Exo70B2 is linked to immune signaling and autophagy
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- Carla Brillada
- Faculty of Biology, Cell Biology, University of Freiburg, 79104 Freiburg, Germany
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- Ooi-Kock Teh
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Franck Anicet Ditengou
- Faculty of Biology, Cell Biology, University of Freiburg, 79104 Freiburg, Germany
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- Chil-Woo Lee
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Till Klecker
- Institute of Cell Biology, University of Bayreuth, 95440 Bayreuth, Germany
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- Bushra Saeed
- Faculty of Biology, Cell Biology, University of Freiburg, 79104 Freiburg, Germany
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- Giulia Furlan
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Marco Zietz
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Gerd Hause
- Biozentrum, Martin-Luther-University Halle-Wittenberg, Halle 06120 (Saale), Germany
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- Lennart Eschen-Lippold
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Wolfgang Hoehenwarter
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Justin Lee
- Leibniz Institute of Plant Biochemistry, 06120 Halle (Saale), Germany
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- Thomas Ott
- Faculty of Biology, Cell Biology, University of Freiburg, 79104 Freiburg, Germany
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- Marco Trujillo
- Faculty of Biology, Cell Biology, University of Freiburg, 79104 Freiburg, Germany
説明
<jats:title>Abstract</jats:title><jats:p>During the immune response, activation of the secretory pathway is key to mounting an effective response, while gauging its output is important to maintain cellular homeostasis. The Exo70 subunit of the exocyst functions as a spatiotemporal regulator by mediating numerous interactions with proteins and lipids. However, a molecular understanding of the exocyst regulation remains challenging. We show that, in Arabidopsis thaliana, Exo70B2 behaves as a bona fide exocyst subunit. Conversely, treatment with the salicylic acid (SA) defence hormone analog benzothiadiazole (BTH), or the immunogenic peptide flg22, induced Exo70B2 transport into the vacuole. We reveal that Exo70B2 interacts with AUTOPHAGY-RELATED PROTEIN 8 (ATG8) via two ATG8-interacting motives (AIMs) and its transport into the vacuole is dependent on autophagy. In line with its role in immunity, we discovered that Exo70B2 interacted with and was phosphorylated by the kinase MPK3. Mimicking phosphorylation had a dual impact on Exo70B2: first, by inhibiting localization at sites of active secretion, and second, it increased the interaction with ATG8. Phosphonull variants displayed higher effector-triggered immunity (ETI) and were hypersensitive to BTH, which induce secretion and autophagy. Our results suggest a molecular mechanism by which phosphorylation diverts Exo70B2 from the secretory into the autophagy pathway for its degradation, to dampen secretory activity.</jats:p>
収録刊行物
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- The Plant Cell
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The Plant Cell 33 (2), 404-419, 2020-12-03
Oxford University Press (OUP)
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キーワード
- Mitogen-Activated Protein Kinase Kinases
- 571
- Virulence
- Arabidopsis Proteins
- Amino Acid Motifs
- Cell Membrane
- Arabidopsis
- Vesicular Transport Proteins
- Pseudomonas syringae
- Models, Biological
- Protein Subunits
- Protein Transport
- Thiadiazoles
- Vacuoles
- Autophagy
- Amino Acid Sequence
- Phosphorylation
- Protein Binding
- Signal Transduction
- trans-Golgi Network
詳細情報 詳細情報について
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- CRID
- 1360853567781435264
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- ISSN
- 1532298X
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- PubMed
- 33630076
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- データソース種別
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- Crossref
- KAKEN
- OpenAIRE