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Review
. 2014 Apr 16;4(4):140017.
doi: 10.1098/rsob.140017.

Polar delivery in plants; commonalities and differences to animal epithelial cells

Urszula Kania  1 , Matyaš Fendrych, Jiři Friml
Affiliations
Review

Polar delivery in plants; commonalities and differences to animal epithelial cells

Urszula Kania et al. Open Biol. .

Abstract

Although plant and animal cells use a similar core mechanism to deliver proteins to the plasma membrane, their different lifestyle, body organization and specific cell structures resulted in the acquisition of regulatory mechanisms that vary in the two kingdoms. In particular, cell polarity regulators do not seem to be conserved, because genes encoding key components are absent in plant genomes. In plants, the broad knowledge on polarity derives from the study of auxin transporters, the PIN-FORMED proteins, in the model plant Arabidopsis thaliana. In animals, much information is provided from the study of polarity in epithelial cells that exhibit basolateral and luminal apical polarities, separated by tight junctions. In this review, we summarize the similarities and differences of the polarization mechanisms between plants and animals and survey the main genetic approaches that have been used to characterize new genes involved in polarity establishment in plants, including the frequently used forward and reverse genetics screens as well as a novel chemical genetics approach that is expected to overcome the limitation of classical genetics methods.

Keywords: PIN proteins; epithelial cells; polarity; screen.

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Figures

Figure 1.
Figure 1.
Schematic of polar domains in the plant epidermal and animal epithelial cells. Plant epidermal cells exhibit four polar domains, apical, basal, inner lateral and outer lateral, and are surrounded by cell walls. Animal epithelial cells exhibit apical and basolateral domains separated by tight junctions.
Figure 2.
Figure 2.
Intracellular trafficking and cellular requirements for polarization of PIN proteins. Auxin binding to its receptor ABP1 inhibits clathrin-mediated endocytosis (CME) through ROP6/RIC4 signalling. PIN proteins require the DRP1 function for CME. They are internalized to the TGN/EE and then follow the pathway to the RE that is regulated by BEN1 and VPS45/BEN2 ARF-GEFs. Recycling of PIN proteins from the RE to the PM is regulated by a GNOM-dependent mechanism. Control of apical and basal PIN targeting depends on the phosphorylation status of PIN proteins. PIN proteins are directed to the apical domain through phosphorylation by PID/WAG1/WAG2 kinases, whereas they are guided to the basal domain by dephosphorylation by means of PP2A/FyPP1/FyPP3 phosphatases. Basal targeting of PIN cargoes is controlled by GNOM. BFA, brefeldin A.
Figure 3.
Figure 3.
Design of a specific screen for PIN polarity components. PIN2 proteins localize to the apical side of epidermal cells in the gravitropic wild-type line. In the pin2 mutant, PIN2 proteins do not occur, provoking the agravitropic phenotype. PIN1-HA is mislocalized in the epidermis to the basal cell side in the PIN2::PIN1-HA;pin2 line, resulting in an agravitropic phenotype. Mutations in the putative PIN polarity regulators (repp) are predicted to restore the apical localization of PIN1 and, hence, the gravitropic phenotype.
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