Abstract

Protein function can be modulated by phase transitions in their material properties, which can range from liquid- to solid-like; yet, the mechanisms that drive these transitions and whether they are important for physiology are still unknown. In the model plant Arabidopsis, we show that developmental robustness is reinforced by phase transitions of the plasma membrane-bound lipid-binding protein SEC14-like. Using imaging, genetics, and in vitro reconstitution experiments, we show that SEC14-like undergoes liquid-like phase separation in the root stem cells. Outside the stem cell niche, SEC14-like associates with the caspase-like protease separase and conserved microtubule motors at unique polar plasma membrane interfaces. In these interfaces, SEC14-like undergoes processing by separase, which promotes its liquid-to-solid transition. This transition is important for root development, as lines expressing an uncleavable SEC14-like variant or mutants of separase and associated microtubule motors show similar developmental phenotypes. Furthermore, the processed and solidified but not the liquid form of SEC14-like interacts with and regulates the polarity of the auxin efflux carrier PINFORMED2. This work demonstrates that robust development can involve liquid-to-solid transitions mediated by proteolysis at unique plasma membrane interfaces.The mechanisms that drive protein phase transitions are unclear. This study in plants shows that an intracellular liquid condensate formed by the lipid transferase SFH8 associates with membranes; when a short fragment of SFH8 is removed by the caspase-like protease ESP, it transforms into a solid filament that can modulate root development.

Published in

PLoS Biology
2023, Volume: 21, number: 9, article number: e3002305
Publisher: PUBLIC LIBRARY SCIENCE

SLU Authors

• Liu, Chen

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    
  • Foundation for Research and Technology - Hellas (FORTH)
  • University of Crete

• Moschou, Panagiotis Nikolaou

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    
  • Foundation for Research and Technology - Hellas (FORTH)
  • University of Crete

UKÄ Subject classification

Biochemistry and Molecular Biology
Plant Biotechnology


Publication identifier

DOI: https://doi.org/10.1371/journal.pbio.3002305

Permanent link to this page (URI)

https://res.slu.se/id/publ/126444