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• W1986687478 abstract "Plant Rho-like small GTPases, usually called ROPs or RACs, function as crucial molecular signal switches in regulating diverse cellular and developmental processes. Once activated by external signals, ROPs interact with their downstream effector proteins, and thus relay signals to downstream targets and initiate a variety of cellular responses such as cytoskeletal organization, vesicle trafficking, secondary cell wall patterning, and cell polarization and morphogenesis (Chen and Friml, 2014Chen X. Friml J. Rho-GTPase-regulated vesicle trafficking in plant cell polarity.Biochem. Soc. Trans. 2014; 42: 212-218Crossref PubMed Scopus (18) Google Scholar). Yet, the mechanisms by which ROP-based signaling participates in regulating these processes are less well known. The phytohormone auxin plays an important role in the versatile aspects of plant developmental and growth processes. These processes are largely dependent on the differential distribution of local auxin gradient that is created by both locally regulating its biosynthesis and polar auxin transport. Polar auxin transport is mainly mediated by auxin carriers, such as members of the PIN-FORMED (PIN) family of auxin efflux carriers, the AUX/LAX family of auxin importers, and ATP-binding cassette transporters subfamily B (ABCB). PIN proteins have been most prominently implicated in the auxin-mediated developmental processes, yet the molecular mechanism underlying the polarization and subcellular trafficking of PIN proteins remains poorly understood. In this Spotlight, we highlight and discuss recent advances in dissecting the emerging but important roles of ROP GTPases in PIN protein polarization. PIN proteins undergo constitutive endocytosis into the endosomal compartments and recycling to the plasma membrane. Auxin and AUXIN-BINDING PROTEIN 1 (ABP1) have been implicated in the regulation of PIN proteins endocytosis in root cells (Robert et al., 2010Robert S. Kleine-Vehn J. Barbez E. Sauer M. Paciorek T. Baster P. Vanneste S. Zhang J. Simon S. Covanova M. et al.ABP1 mediates auxin inhibition of clathrin-dependent endocytosis in Arabidopsis.Cell. 2010; 143: 111-121Abstract Full Text Full Text PDF PubMed Scopus (325) Google Scholar). In the jigsaw-puzzle appearance of leaf pavement cells, ABP1 interacts with the transmembrane kinase (TMK) receptor-like kinase to form the auxin-sensing complex and thereby mediates auxin signaling to coordinately activate two mutually exclusive ROP2 and ROP6 signaling pathways (Xu et al., 2014Xu T. Dai N. Chen J. Nagawa S. Cao M. Li H. Zhou Z. Chen X. De Rycke R. Rakusova H. et al.Cell surface ABP1-TMK auxin-sensing complex activates ROP GTPase signaling.Science. 2014; 343: 1025-1028Crossref PubMed Scopus (205) Google Scholar). Both ROP2 and PIN1 are preferentially localized to the lobe tips of young pavement cells, and rop2 rop4RNAi mutants and pin1-1 mutants cause similar defective interdigitation of pavement cells (Xu et al., 2010Xu T. Wen M. Nagawa S. Fu Y. Chen J. Wu M. Perrot-Rechenmann C. Friml J. Jones A.M. Yang Z. Cell surface- and Rho GTPase-based auxin signaling controls cellular interdigitation in Arabidopsis.Cell. 2010; 143: 99-110Abstract Full Text Full Text PDF PubMed Scopus (359) Google Scholar). PIN1 endocytosis occurs at the indentation regions but is inhibited within the lobe regions. In the lobe regions, lobe tip-localized ROP2 mediates the inhibition of PIN1 internalization into the endosomal compartments. ROP2 interacts with one of its effectors, ROP Interactive CRIB motif-containing protein 4 (RIC4), and thus promotes the assembly of fine cortical microfilaments, leading to the inhibition of PIN1 endocytosis (Nagawa et al., 2012Nagawa S. Xu T. Lin D. Dhonukshe P. Zhang X. Friml J. Scheres B. Fu Y. Yang Z. ROP GTPase-dependent actin microfilaments promote PIN1 polarization by localized inhibition of clathrin-dependent endocytosis.PLoS Biol. 2012; 10: e1001299Crossref PubMed Scopus (161) Google Scholar). Meanwhile, local auxin transported outside by PIN1 to the cell wall activates ROP2 at the lobe regions to form a positive feedback loop for the control of PIN1 polarization. The signaling mechanism of auxin-ABP1-ROP2-RIC4-PIN1 in leaf pavement cells provides a feedback regulation for ROP2 activation. In Arabidopsis root cells, the signaling mechanisms involved in PIN proteins polarization are similar to the coordination of the polarity in leaf pavement cells. ROP6 and its downstream effector negatively regulate clathrin-mediated endocytosis of both PIN1 and PIN2, and as a consequence have an effect on corresponding auxin transport-mediated processes, such as lateral root patterning and root gravitropism (Chen et al., 2012Chen X. Naramoto S. Robert S. Tejos R. Lofke C. Lin D. Yang Z. Friml J. ABP1 and ROP6 GTPase signaling regulate clathrin-mediated endocytosis in Arabidopsis roots.Curr. Biol. 2012; 22: 1326-1332Abstract Full Text Full Text PDF PubMed Scopus (130) Google Scholar, Lin et al., 2012Lin D. Nagawa S. Chen J. Cao L. Chen X. Xu T. Li H. Dhonukshe P. Yamamuro C. Friml J. et al.A ROP GTPase-dependent auxin signaling pathway regulates the subcellular distribution of PIN2 in Arabidopsis roots.Curr. Biol. 2012; 22: 1319-1325Abstract Full Text Full Text PDF PubMed Scopus (146) Google Scholar). Through a genetic screen, Lin and colleagues found that SPIKE1, which belongs to the dock homology region 2 (DHR2)-type of RhoGEF, interacts with ROP6 and is required for auxin activation of ROP6 in the control of PIN2 subcellular localization (Lin et al., 2012Lin D. Nagawa S. Chen J. Cao L. Chen X. Xu T. Li H. Dhonukshe P. Yamamuro C. Friml J. et al.A ROP GTPase-dependent auxin signaling pathway regulates the subcellular distribution of PIN2 in Arabidopsis roots.Curr. Biol. 2012; 22: 1319-1325Abstract Full Text Full Text PDF PubMed Scopus (146) Google Scholar). Mutants of spk1 roots have increased PIN2 internalization, just as observed in rop6 and ric1 mutants. Genetic data have revealed that the ROP6-RIC1 pathway acts downstream of ABP1 to regulate endocytosis (Chen et al., 2012Chen X. Naramoto S. Robert S. Tejos R. Lofke C. Lin D. Yang Z. Friml J. ABP1 and ROP6 GTPase signaling regulate clathrin-mediated endocytosis in Arabidopsis roots.Curr. Biol. 2012; 22: 1326-1332Abstract Full Text Full Text PDF PubMed Scopus (130) Google Scholar). However, the connection between ABP1 and SPIKE1 remains unclear. It is reasonable to hypothesize that the ABP1-TMK1 auxin-sensing complex may interact with SPIKE1 to transmit the auxin signal to ROPs and downstream targets for inducing PIN proteins endocytosis. The evidence implying that ROPs may participate in exocytosis came from the identification of the Interactor of Constitutive Active ROP (ICR) or ROP Interactive Partner (RIP) family members as the effectors of ROP6 and ROP10 (Lavy et al., 2007Lavy M. Bloch D. Hazak O. Gutman I. Poraty L. Sorek N. Sternberg H. Yalovsky S. A novel ROP/RAC effector links cell polarity, root-meristem maintenance, and vesicle trafficking.Curr. Biol. 2007; 17: 947-952Abstract Full Text Full Text PDF PubMed Scopus (173) Google Scholar). Loss of ICR1 function leads to defective polarization of PIN1 and PIN2 in root cells, resulting in severe embryo and root defects correlating with a decreased local auxin maximum (Hazak et al., 2010Hazak O. Bloch D. Poraty L. Sternberg H. Zhang J. Friml J. Yalovsky S. A Rho scaffold integrates the secretory system with feedback mechanisms in regulation of auxin distribution.PLoS Biol. 2010; 8: e1000282Crossref PubMed Scopus (85) Google Scholar). ICR1 binds to the exocyst complex subunit SEC3 and is proposed to be involved in the regulation of PIN proteins to the plasma membrane polar domains in roots. The icr1 mutant also has leaf pavement cell phenotypes with small and cubical cells. Overexpression of ICR1 leads to loss of the interdigitated appearance of pavement cells, similar to the phenotypes of overexpressing constitutively active ROP6. However, whether ICR1-mediated ROP signaling is required for PIN1 recycling to the plasma membrane of the lobe tips remains unknown. More recently, ROP3 has been found to be required for the recycling of PIN1 and PIN3 to the plasma membrane in root cells (Huang et al., 2014Huang J. Liu H. Chen M. Li X. Wang M. Yang Y. Wang C. Huang J. Liu G. Liu Y. et al.ROP3 GTPase contributes to polar auxin transport and auxin responses and is important for embryogenesis and seedling growth in Arabidopsis.Plant Cell. 2014; 26: 3501-3518Crossref PubMed Scopus (43) Google Scholar). Both ROP3 loss of function and ectopic expression of dominant negative ROP3 lead to aberrant division patterns in embryos and severe defective postembryonic organ formation, which is caused by a significantly reduced auxin maximum. In both DN-rop3 and rop3 mutant embryos, PIN1-GFP localization to the plasma membrane is decreased, and is found in intracellular aggregates. In roots, the polar localization of both PIN1-GFP and PIN3-GFP but not PIN2-GFP is changed, partially showing a basal-to-apical shift. By using the washout of brefeldin A, ROP3 was found to have no effect on the endocytosis of PIN proteins, but it is required for the regulation of the exocytosis of PIN1 or PIN3 to the plasma membrane. However, the signaling mechanism underling ROP3 regulation of PIN protein trafficking is elusive. It is necessary to investigate whether or not auxin is required for the activation of ROP3. Furthermore, it is worth testing the connection between ROP3 and ICR1 because both are required for the recycling of PIN1 to the plasma membrane in roots. ROP GTPases function as key regulators of cell polarity in plants. Recent studies have suggested that ROP GTPase-dependent auxin signaling in the regulation of PIN protein trafficking mediated by endocytosis and exocytosis is the mechanism responsible for the control of polar auxin transport in Arabidopsis. These findings have also implied a positive feedback signaling mechanism for the subcellular trafficking of PIN proteins. The current working model for the subcellular trafficking of PIN proteins mediated by ROP GTPases is shown in Figure 1. We are still far from understanding the specific roles of ROP upstream and downstream components in the regulation of endocytosis or exocytosis. As important upstream modulators, TMK family members have been shown to activate ROP signaling (Xu et al., 2014Xu T. Dai N. Chen J. Nagawa S. Cao M. Li H. Zhou Z. Chen X. De Rycke R. Rakusova H. et al.Cell surface ABP1-TMK auxin-sensing complex activates ROP GTPase signaling.Science. 2014; 343: 1025-1028Crossref PubMed Scopus (205) Google Scholar). In the future, it would be interesting to study the possible roles of these receptor-like kinases in ROP-regulated PIN trafficking. Previous studies have suggested that the organization of F-actin is important for PIN trafficking and polarity, however, the specific mechanism underlying this process is poorly understood. The cortical microtubule organization has been implicated in the regulation of PIN2 trafficking (Ambrose et al., 2013Ambrose C. Ruan Y. Gardiner J. Tamblyn L.M. Catching A. Kirik V. Marc J. Overall R. Wasteneys G.O. CLASP interacts with sorting nexin 1 to link microtubules and auxin transport via PIN2 recycling in Arabidopsis thaliana.Dev. Cell. 2013; 24: 649-659Abstract Full Text Full Text PDF PubMed Scopus (113) Google Scholar). Future studies should investigate whether or not the microtubule-severing enzyme katanin, a downstream target of ROP6-RIC1 signaling (Lin et al., 2013Lin D. Cao L. Zhou Z. Zhu L. Ehrhardt D. Yang Z. Fu Y. Rho GTPase signaling activates microtubule severing to promote microtubule ordering in Arabidopsis.Curr. Biol. 2013; 23: 290-297Abstract Full Text Full Text PDF PubMed Scopus (151) Google Scholar), is required for PIN polarization. Meanwhile, it is useful to identify new components involved in ROP signaling to better understand the signaling mechanisms in the regulation of endocytosis and exocytosis in plants. This work was supported by startup funds to D.L. from the Center for Genomics and Biotechnology, Fujian Agriculture and Forestry University." @default.
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• W1986687478 title "ROP GTPase Regulation of Auxin Transport in Arabidopsis" @default.
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