Sammanfattning

Cellular condensates can comprise membrane-less ribonucleoprotein assemblies with liquid-like properties. These cellular condensates influence various biological outcomes, but their liquidity hampers their isolation and characterization. Here, we investigated the composition of the condensates known as processing bodies (PBs) in the model plant Arabidopsis thaliana through a proximity-biotinylation proteomics approach. Using in situ protein-protein interaction approaches, genetics and high-resolution dynamic imaging, we show that processing bodies comprise networks that interface with membranes. Surprisingly, the conserved component of PBs, DECAPPING PROTEIN 1 (DCP1), can localize to unique plasma membrane subdomains including cell edges and vertices. We characterized these plasma membrane interfaces and discovered a developmental module that can control cell shape. This module is regulated by DCP1, independently from its role in decapping, and the actin-nucleating SCAR-WAVE complex, whereby the DCP1-SCAR-WAVE interaction confines and enhances actin nucleation. This study reveals an unexpected function for a conserved condensate at unique membrane interfaces.

Nyckelord

ARP2-ARP3; condensates; LLPS; plasma membrane domains; SCAR-WAVE

Publicerad i

EMBO Journal
2023, Volym: 42, nummer: 9
Utgivare: WILEY

SLU författare

• Liu, Chen

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    

• Muhammad, Amna

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    
  • Pir Mehr Ali Shah Arid Agriculture University

• Moschou, Panagiotis Nikolaou

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    
  • Foundation for Research and Technology - Hellas (FORTH)
  • Πανεπιστήμιο Κρήτης

Associerade SLU-program

SLU Nätverk växtskydd


UKÄ forskningsämne

Cellbiologi


Publikationens identifierare

DOI: https://doi.org/10.15252/embj.2022111885

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/121504