Arp2/3 Complex Is Required for Auxin-Driven Cell Expansion Through Regulation of Auxin Transporter Homeostasis

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...

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Bibliographic Details
Main Authors: Judith García-González, Štépánka Kebrlová, Matěj Semerák, Jozef Lacek, Innu Kotannal Baby, Jan Petrášek, Kateřina Schwarzerová
Format: Article
Language:English
Published: Frontiers Media S.A. 2020-04-01
Series:Frontiers in Plant Science
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Online Access:https://www.frontiersin.org/article/10.3389/fpls.2020.00486/full
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Summary: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.
ISSN:1664-462X