Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants
- Author
- Jonathan Dragwidge (UGent) , Yanning Wang, Lysiane Brocard, Andreas De Meyer (UGent) , Roman Hudeček, Dominique Eeckhout (UGent) , Peter Grones (UGent) , Matthieu Buridan, Clément Chambaud, Přemysl Pejchar, Martin Potocký, Joanna Winkler, Michaël Vandorpe (UGent) , Nelson Serre, Matyáš Fendrych, Amelie Bernard, Geert De Jaeger (UGent) , Roman Pleskot, Xiaofeng Fang and Daniël Van Damme (UGent)
- Organization
- Project
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- ZAP-ambt in het kader van ERC-project T-REX
- Dominant negative modulation of plant endocytosis to identify fast-cycling cargoes of the TPLATE and AP-2 adaptor complexes
- Kinase-dependent regulation of plant endocytosis upon temperature stress.
- Functional and structural characterization of the appendage domains of the large endocytic adaptors in plants to achieve a mechanistic understanding of their differential role.
- Abstract
- Clathrin-mediated endocytosis is an essential cellular internalization pathway involving the dynamic assembly of clathrin and accessory proteins to form membrane-bound vesicles. The evolutionarily ancient TSET–TPLATE complex (TPC) plays an essential, but ill-defined role in endocytosis in plants. Here we show that two highly disordered TPC subunits, AtEH1 and AtEH2, function as scaffolds to drive biomolecular condensation of the complex. These condensates specifically nucleate on the plasma membrane through interactions with anionic phospholipids, and facilitate the dynamic recruitment and assembly of clathrin, as well as early- and late-stage endocytic accessory proteins. Importantly, condensation promotes ordered clathrin assemblies. TPC-driven biomolecular condensation thereby facilitates dynamic protein assemblies throughout clathrin-mediated endocytosis. Furthermore, we show that a disordered region of AtEH1 controls the material properties of endocytic condensates in vivo. Alteration of these material properties disturbs the recruitment of accessory proteins, influences endocytosis dynamics and impairs plant responsiveness. Our findings reveal how collective interactions shape endocytosis.
- Keywords
- Cell Biology, PHASE-SEPARATION, SOMATIC CYTOKINESIS, PROTEINS, TPLATE, REVEALS, DRP1A, ESTABLISHMENT, RECRUITMENT, BIOLOGY, ADAPTER
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-01HQ5NQAJQM2CNFVX40FZ6NK9W
- MLA
- Dragwidge, Jonathan, et al. “Biomolecular Condensation Orchestrates Clathrin-Mediated Endocytosis in Plants.” NATURE CELL BIOLOGY, vol. 26, no. 3, 2024, pp. 438–49, doi:10.1038/s41556-024-01354-6.
- APA
- Dragwidge, J., Wang, Y., Brocard, L., De Meyer, A., Hudeček, R., Eeckhout, D., … Van Damme, D. (2024). Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants. NATURE CELL BIOLOGY, 26(3), 438–449. https://doi.org/10.1038/s41556-024-01354-6
- Chicago author-date
- Dragwidge, Jonathan, Yanning Wang, Lysiane Brocard, Andreas De Meyer, Roman Hudeček, Dominique Eeckhout, Peter Grones, et al. 2024. “Biomolecular Condensation Orchestrates Clathrin-Mediated Endocytosis in Plants.” NATURE CELL BIOLOGY 26 (3): 438–49. https://doi.org/10.1038/s41556-024-01354-6.
- Chicago author-date (all authors)
- Dragwidge, Jonathan, Yanning Wang, Lysiane Brocard, Andreas De Meyer, Roman Hudeček, Dominique Eeckhout, Peter Grones, Matthieu Buridan, Clément Chambaud, Přemysl Pejchar, Martin Potocký, Joanna Winkler, Michaël Vandorpe, Nelson Serre, Matyáš Fendrych, Amelie Bernard, Geert De Jaeger, Roman Pleskot, Xiaofeng Fang, and Daniël Van Damme. 2024. “Biomolecular Condensation Orchestrates Clathrin-Mediated Endocytosis in Plants.” NATURE CELL BIOLOGY 26 (3): 438–449. doi:10.1038/s41556-024-01354-6.
- Vancouver
- 1.Dragwidge J, Wang Y, Brocard L, De Meyer A, Hudeček R, Eeckhout D, et al. Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants. NATURE CELL BIOLOGY. 2024;26(3):438–49.
- IEEE
- [1]J. Dragwidge et al., “Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants,” NATURE CELL BIOLOGY, vol. 26, no. 3, pp. 438–449, 2024.
@article{01HQ5NQAJQM2CNFVX40FZ6NK9W,
abstract = {{Clathrin-mediated endocytosis is an essential cellular internalization pathway involving the dynamic assembly of clathrin and accessory proteins to form membrane-bound vesicles. The evolutionarily ancient TSET–TPLATE complex (TPC) plays an essential, but ill-defined role in endocytosis in plants. Here we show that two highly disordered TPC subunits, AtEH1 and AtEH2, function as scaffolds to drive biomolecular condensation of the complex. These condensates specifically nucleate on the plasma membrane through interactions with anionic phospholipids, and facilitate the dynamic recruitment and assembly of clathrin, as well as early- and late-stage endocytic accessory proteins. Importantly, condensation promotes ordered clathrin assemblies. TPC-driven biomolecular condensation thereby facilitates dynamic protein assemblies throughout clathrin-mediated endocytosis. Furthermore, we show that a disordered region of AtEH1 controls the material properties of endocytic condensates in vivo. Alteration of these material properties disturbs the recruitment of accessory proteins, influences endocytosis dynamics and impairs plant responsiveness. Our findings reveal how collective interactions shape endocytosis.}},
author = {{Dragwidge, Jonathan and Wang, Yanning and Brocard, Lysiane and De Meyer, Andreas and Hudeček, Roman and Eeckhout, Dominique and Grones, Peter and Buridan, Matthieu and Chambaud, Clément and Pejchar, Přemysl and Potocký, Martin and Winkler, Joanna and Vandorpe, Michaël and Serre, Nelson and Fendrych, Matyáš and Bernard, Amelie and De Jaeger, Geert and Pleskot, Roman and Fang, Xiaofeng and Van Damme, Daniël}},
issn = {{1465-7392}},
journal = {{NATURE CELL BIOLOGY}},
keywords = {{Cell Biology,PHASE-SEPARATION,SOMATIC CYTOKINESIS,PROTEINS,TPLATE,REVEALS,DRP1A,ESTABLISHMENT,RECRUITMENT,BIOLOGY,ADAPTER}},
language = {{eng}},
number = {{3}},
pages = {{438--449}},
title = {{Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants}},
url = {{http://doi.org/10.1038/s41556-024-01354-6}},
volume = {{26}},
year = {{2024}},
}
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