An actin remodeling role for Arabidopsis processing bodies revealed by their proximity interactome

Chen Liu, Andriani Mentzelopoulou, Amna Muhammad, Andriy Volkov, Dolf Weijers, Emilio Gutierrez-Beltran, Panagiotis N. Moschou*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Article numbere111885
Number of pages26
JournalEMBO Journal
Issue number9
Early online date6 Feb 2023
Publication statusPublished - 2 May 2023


  • ARP2–ARP3
  • condensates
  • LLPS
  • plasma membrane domains


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