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

0531597 - ÚEB 2021 RIV CH eng J - Journal Article
García-González, J. - Kebrlová, Š. - Semerák, M. - Lacek, Jozef - Kotannal Baby, I. - Petrášek, J. - Schwarzerová, K.
Arp2/3 Complex Is Required for Auxin-Driven Cell Expansion Through Regulation of Auxin Transporter Homeostasis.
Frontiers in Plant Science. Roč. 11, APR 28 (2020), č. článku 486. ISSN 1664-462X. E-ISSN 1664-462X
R&D Projects: GA MŠMT(CZ) LM2015062
Institutional support: RVO:61389030
Keywords : actin * Arp2/3 complex * auxin * cell expansion * cytoskeleton
OECD category: Biochemistry and molecular biology
Impact factor: 5.754, year: 2020
Method of publishing: Open access
http://doi.org/10.3389/fpls.2020.00486

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.
Permanent Link: http://hdl.handle.net/11104/0310229