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Arp2/3 Complex Is Required for Auxin-Driven Cell Expansion Through Regulation of Auxin Transporter Homeostasis
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SYSNO ASEP 0531597 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Arp2/3 Complex Is Required for Auxin-Driven Cell Expansion Through Regulation of Auxin Transporter Homeostasis Author(s) García-González, J. (CZ)
Kebrlová, Š. (CZ)
Semerák, M. (CZ)
Lacek, Jozef (UEB-Q) ORCID
Kotannal Baby, I. (CZ)
Petrášek, J. (CZ)
Schwarzerová, K. (CZ)Number of authors 7 Article number 486 Source Title Frontiers in Plant Science. - : Frontiers Research Foundation - ISSN 1664-462X
Roč. 11, APR 28 (2020)Number of pages 15 s. Language eng - English Country CH - Switzerland Keywords actin ; Arp2/3 complex ; auxin ; cell expansion ; cytoskeleton Subject RIV EB - Genetics ; Molecular Biology OECD category Biochemistry and molecular biology R&D Projects LM2015062 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UEB-Q - RVO:61389030 UT WOS 000536079500001 EID SCOPUS 85084539035 DOI 10.3389/fpls.2020.00486 Annotation The Arp2/3 complex is an actin nucleator shown to be required throughout plant morphogenesis, contributing to processes such as cell expansion, tissue differentiation or cell wall assembly. A recent publication demonstrated that plants lacking functional Arp2/3 complex also present defects in auxin distribution and transport. This work shows that Arp2/3 complex subunits are predominantly expressed in the provasculature, although other plant tissues also show promoter activity (e.g., cotyledons, apical meristems, or root tip). Moreover, auxin can trigger subunit expression, indicating a role of this phytohormone in mediating the complex activity. Further investigation of the functional interaction between Arp2/3 complex and auxin signaling also reveals their cooperation in determining pavement cell shape, presumably through the role of Arp2/3 complex in the correct auxin carrier trafficking. Young seedlings of arpc5 mutants show increased auxin-triggered proteasomal degradation of DII-VENUS and altered PIN3 distribution, with higher levels of the protein in the vacuole. Closer observation of vacuolar morphology revealed the presence of a more fragmented vacuolar compartment when Arp2/3 function is abolished, hinting a generalized role of Arp2/3 complex in endomembrane function and protein trafficking. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2021 Electronic address http://doi.org/10.3389/fpls.2020.00486
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