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ARP2/3 complex associates with peroxisomes to participate in pexophagy in plants
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SYSNO ASEP 0578504 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title ARP2/3 complex associates with peroxisomes to participate in pexophagy in plants Author(s) Martínek, J. (CZ)
Cifrová, P. (CZ)
Vosolsobě, S. (CZ)
García-González, J. (CZ)
Malínská, Kateřina (UEB-Q) RID, ORCID
Mauerová, Z. (CZ)
Jelínková, B. (CZ)
Krtková, J. (CZ)
Sikorová, L. (CZ)
Leaves, I. (GB)
Sparkes, I. (GB)
Schwarzerová, K. (CZ)Number of authors 12 Source Title Nature Plants - ISSN 2055-026X
Roč. 9, č. 11 (2023), s. 1874-1889Number of pages 16 s. Language eng - English Country GB - United Kingdom Keywords ACTIN CYTOSKELETON ; CELL-SHAPE ; PROTEIN2/3 COMPLEX OECD category Cell biology R&D Projects LM2023050 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UEB-Q - RVO:61389030 UT WOS 001085866900002 EID SCOPUS 85174296475 DOI 10.1038/s41477-023-01542-6 Annotation 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. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2024 Electronic address https://doi.org/10.1038/s41477-023-01542-6
Number of the records: 1