ARP2/3 complex associates with peroxisomes to participate in pexophagy in plants

0578504 - ÚEB 2024 RIV GB eng J - Journal Article
Martínek, J. - Cifrová, P. - Vosolsobě, S. - García-González, J. - Malínská, Kateřina - Mauerová, Z. - Jelínková, B. - Krtková, J. - Sikorová, L. - Leaves, I. - Sparkes, I. - Schwarzerová, K.
ARP2/3 complex associates with peroxisomes to participate in pexophagy in plants.
Nature Plants. Roč. 9, č. 11 (2023), s. 1874-1889. ISSN 2055-026X. E-ISSN 2055-0278
R&D Projects: GA MŠMT(CZ) LM2023050
Institutional support: RVO:61389030
Keywords : ACTIN CYTOSKELETON * CELL-SHAPE * PROTEIN2/3 COMPLEX
OECD category: Cell biology
Impact factor: 18, year: 2022
Method of publishing: Open access
https://doi.org/10.1038/s41477-023-01542-6

Actin-related protein (ARP2/3) complex is a heteroheptameric protein complex, evolutionary conserved in all eukaryotic organisms. Its conserved role is based on the induction of actin polymerization at the interface between membranes and the cytoplasm. Plant ARP2/3 has been reported to participate in actin reorganization at the plasma membrane during polarized growth of trichomes and at the plasma membrane–endoplasmic reticulum contact sites. Here we demonstrate that individual plant subunits of ARP2/3 fused to fluorescent proteins form motile spot-like structures in the cytoplasm that are associated with peroxisomes in Arabidopsis and tobacco. ARP2/3 is found at the peroxisome periphery and contains the assembled ARP2/3 complex and the WAVE/SCAR complex subunit NAP1. This ARP2/3-positive peroxisomal domain colocalizes with the autophagosome and, under conditions that affect the autophagy, colocalization between ARP2/3 and the autophagosome increases. ARP2/3 subunits co-immunoprecipitate with ATG8f and peroxisome-associated ARP2/3 interact in vivo with the ATG8f marker. Since mutants lacking functional ARP2/3 complex have more peroxisomes than wild type, we suggest that ARP2/3 has a novel role in the process of peroxisome degradation by autophagy, called pexophagy.
Permanent Link: https://hdl.handle.net/11104/0347490