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High soil salinity constitutes a major environmental constraint to crop production worldwide, and the identification of genetic determinants of plant salt tolerance is awaited by breeders. While the leaf K+ to Na+ homeostasis is considered as key parameter of plant salt tolerance, the underlying mechanisms are not fully identified. Especially, the contribution of K+ channels to this homeostasis has been scarcely examined. Here, we show, using a reverse genetics approach, that the outwardly-rectifying K+ channel OsK5.2, involved in K+ translocation to the shoot and K+ release by guard cells for stomatal closure, is a strong determinant of rice salt tolerance. Upon saline treatment, OsK5.2 function in xylem sap K+ load was maintained, and even transiently increased, in roots. OsK5.2 selectively handled K+ in roots and was not involved in xylem sap Na+ load. In shoots, OsK5.2 expression was up-regulated from the onset of the saline treatment, enabling fast reduction of stomatal aperture, decreased transpirational water flow and therefore decreased trans-plant Na+ flux and reduced leaf Na+ accumulation. Thus, the OsK5.2 functions allowed shoot K+ nutrition while minimizing arrival of Na+, and appeared highly beneficial to the leaf K+ to Na+ homeostasis, the avoidance of salt toxicity and plant growth maintaining.

Aquaporins transport water and small neutral molecules across different membranes in plant cells and thus play important roles in cellular and whole plant physiology. The high diversity of intracellular localization of aquaporin isoforms is dependent on specific trafficking machineries. ER-to-Golgi trafficking of the plasma membrane intrinsic protein (PIP) isoforms has been shown to be dependent on DxE motifs in N-terminal cytosolic region, LxxxA motif in transmembrane domain 3, phosphorylation in C-terminal cytosolic region, and heteromerization. Stress-induced downregulation of the PIPs in the early secretory pathway was uncovered. Subsets of PIPs and Nodulin 26-like intrinsic proteins (NIPs) showed polar localization in the plasma membrane (PM) in certain cell types for directional transport of water and small neutral molecules such as boric acid and silicic acid. Latest techniques to study the mobility of PIPs revealed immobile nature in the plane of the PM and constitutive cycling between the PM and the endosomes. The roles of clathrin- and microdomain-dependent endocytosis for PIPs were uncovered. When challenged by stress conditions, some PIPs and TIPs showed quick relocalization probably to adjust water status. Vacuolar trafficking of different TIPs was shown to follow multiple routes dependent or independent of Golgi apparatus. These findings greatly advanced our understanding of the trafficking machineries of plant aquaporins, as significant models of plant membrane proteins.

The nano-mixed oxides CeO2-TiO2 was synthesized by gel combustion method using polyvinyl alcohol as fuel and mixtures of titanium trichloride and cerium(IV) nitrate at a relatively low calcination temperature of 550°C for 2 h. The prepared CeO2-TiO2 nanoparticles with a specific area of 65.70 m2 g−1 were dispersed in polyurethane matrix in different concentration conditions from 0.0 to 1.5 wt% to study ultraviolet durability following HONDA HES D 6501-97 standards. After 400 h of testing in the QUV accelerate weathering tester, the thin film containing 1 wt% CeO2-TiO2 nano-mixed oxides has presented the noticeable capacity for absorbing ultraviolet light by only 6.8 g.u change in specular gloss at 60° and ΔE = 3.66 in color difference.

Aquaporins (AQPs) are channel proteins that facilitate the transport of water and small solutes across biological membranes. In plants, AQPs exhibit a high multiplicity of isoforms in relation to a high diversity of sub-cellular localizations, at the plasma membrane (PM) and in various intracellular compartments. Some members also exhibit a dual localization in distinct cell compartments, whereas others show polarized or domain-specific expression at the PM or tonoplast, respectively. A diversity of mechanisms controlling the routing of newly synthesized AQPs towards their destination membranes and involving diacidic motifs, phosphorylation or tetramer assembly is being uncovered. Recent approaches using single particle tracking, fluorescence correlation spectroscopy and fluorescence recovery after photobleaching have, in combination with pharmacological interference, stressed the peculiarities of AQP sub-cellular dynamics in environmentally challenging conditions. A role for clathrin and sterol-rich domains in cell surface dynamics and endocytosis of PM AQPs was uncovered. These recent advances provide deep insights into the cellular mechanisms of water transport regulation in plants. They also point to AQPs as an emerging model for studying the sub-cellular dynamics of plant membrane proteins.

This paper presents superpixel-based background removal methods to increase accuracy of global salience person re-identication method. The current algorithm has two problems which limit its accuracy including (1) wrong matching when images of different people have the same background and/or (2) salience on the background of different images of different people is similar. Theoretical maximum accuracy of the global salience method when applying background removal was proved in our previous work by manually remove background close to a human. To achieve an automatic background removal with an accuracy close to the theory, we propose two approaches namely (i) superpixel-GBVS method that combines superpixel and local salience information and (ii) superpixel-pose method that combines superpixel and pose estimation information. The two technologies decide what superpixels belong to human and the others belong to background. It results in a background removal close to edges of the human. Preliminary results show that our results outperform those of the original method without applying any background removal methods and results of the second approach are close to the theory.

The constitutive cycling of plant plasma membrane (PM) proteins is an essential component of their function and regulation under resting or stress conditions. Transgenic Arabidopsis plants that express GFP fusions with AtPIP1;2 and AtPIP2;1, two prototypic PM aquaporins, were used to develop a fluorescence recovery after photobleaching (FRAP) approach. This technique was used to discriminate between PM and endosomal pools of the aquaporin constructs, and to estimate their cycling between intracellular compartments and the cell surface. The membrane trafficking inhibitors tyrphostin A23, naphthalene-1-acetic acid and brefeldin A blocked the latter process. By contrast, a salt treatment (100 mm NaCl for 30 min) markedly enhanced the cycling of the aquaporin constructs and modified their pharmacological inhibition profile. Two distinct models for PM aquaporin cycling in resting or salt-stressed root cells are discussed.

International audience; Aquaporins are channel proteins that facilitate the transport of water and small neutral molecules, including gases, across cell membranes of most of the living organisms. Integrative studies have stressed the role of aquaporins in maintaining the whole plant water and nutrient status. Cellular aspects of plant aquaporin functions and regulations are also extensively investigated. The present review provides a glance at recent progresses in this area. One first direction concerns the mechanisms that determine aquaporin targeting to specific subcellular membranes and a dynamic and stimulus-dependent control of their density in these membranes. The regulation of aquaporin opening and closing and its links to cell signalling cascades are also discussed. Multiple cellular functions are now attributed to plant aquaporins. They include the dynamic equilibration and subcellular partitioning of their various substrates and a contribution to cell expansion and possibly cell division.

The water uptake capacity of plant roots (i.e. their hydraulic conductivity, Lp r ) is determined in large part by aquaporins of the plasma membrane intrinsic protein (PIP) subfamily. In the present work, we investigated two stimuli, salicylic acid (SA) and salt, because of their ability to induce an accumulation of reactive oxygen species (ROS) and an inhibition of Lp r concomitantly in the roots of Arabidopsis plants. The inhibition of Lp r by SA was partially counteracted by preventing the accumulation of hydrogen peroxide (H 2 O 2 ) with exogenous catalase. In addition, exogenous H 2 O 2 was able to reduce Lp r by up to 90% in

Microscopic techniques allow either a global mobility analysis of proteins with fluorescence recovery after photobleaching (FRAP) or single-protein mobility characterization with single-particle or quantum dot tracking. For instance, total internal reflection fluorescence microscopy allowed single-particle tracking (SPT) of Arabidopsis plasma membrane (PM) proteins, revealing their heterogeneous distribution, low lateral diffusion, and dynamic properties in response to salt stress (Li et al., 2011).

Measuring the mobility and interactions of proteins is key to understanding cellular signaling mechanisms; however, quantitative analysis of protein dynamics in living plant cells remains a major challenge. Here we describe an automated, single-molecule protocol based on total internal reflection fluorescence microscopy (TIRFM) imaging that allows protein tracking and subunit counting in living plant cells. This protocol uses TIRFM to image transgenic plant tissues expressing fluorescently tagged proteins that are localized to the plasma membrane. Next, a tracking algorithm quantifies dynamic changes in fluorescent protein motion types, temporary particle displacement and protein photobleaching steps. This protocol allows researchers to study the kinetic characteristics of heterogeneously distributed proteins. The approach has potential applications for studies of protein dynamics and subunit stoichiometry for a wide variety of plasma membrane and intracellular proteins in living plant cells and other biological specimens visualized by TIRFM or other fluorescence imaging techniques. The whole protocol can be completed in 5-6 h.

Aquaporins are membrane channels that facilitate the transport of water and small neutral molecules across biological membranes of most living organisms. In plants, aquaporins occur as multiple isoforms reflecting a high diversity of cellular localizations, transport selectivity, and regulation properties. Plant aquaporins are localized in the plasma membrane, endoplasmic reticulum, vacuoles, plastids and, in some species, in membrane compartments interacting with symbiotic organisms. Plant aquaporins can transport various physiological substrates in addition to water. Of particular relevance for plants is the transport of dissolved gases such as carbon dioxide and ammonia or metalloids such as boron and silicon. Structure-function studies are developed to address the molecular and cellular mechanisms of plant aquaporin gating and subcellular trafficking. Phosphorylation plays a central role in these two processes. These mechanisms allow aquaporin regulation in response to signaling intermediates such as cytosolic pH and calcium, and reactive oxygen species. Combined genetic and physiological approaches are now integrating this knowledge, showing that aquaporins play key roles in hydraulic regulation in roots and leaves, during drought but also in response to stimuli as diverse as flooding, nutrient availability, temperature, or light. A general hydraulic control of plant tissue expansion by aquaporins is emerging, and their role in key developmental processes (seed germination, emergence of lateral roots) has been established. Plants with genetically altered aquaporin functions are now tested for their ability to improve plant tolerance to stresses. In conclusion, research on aquaporins delineates ever expanding fields in plant integrative biology thereby establishing their crucial role in plants.

Aquaporins are water channel proteins that mediate the fine-tuning of cell membrane water permeability during development or in response to environmental stresses. The present work focuses on the oxidative stress-induced redistribution of plasma membrane intrinsic protein (PIP) aquaporins from the plasma membrane (PM) to intracellular membranes. This process was investigated in the Arabidopsis root. Sucrose density gradient centrifugation showed that exposure of roots to 0.5 mM H2O2 induces significant depletion in PM fractions of several abundant PIP homologs after 15 min. Analyses by single-particle tracking and fluorescence correlative spectroscopy showed that, in the PM of epidermal cells, H2O2 treatment induces an increase in lateral motion and a reduction in the density of a fluorescently tagged form of the prototypal AtPIP2;1 isoform, respectively. Co-expression analyses of AtPIP2;1 with endomembrane markers revealed that H2O2 triggers AtPIP2;1 accumulation in the late endosomal compartments. Life-time analyses established that the high stability of PIPs was maintained under oxidative stress conditions, suggesting that H2O2 triggers a mechanism for intracellular sequestration of PM aquaporins without further degradation. In addition to information on cellular regulation of aquaporins, this study provides novel and complementary insights into the dynamic remodeling of plant internal membranes during oxidative stress responses.

The aim of this paper is to study a deep connection between local cohomology annihilators and Macaulayfication and arithmetic Macaulayfication over a local ring. Local cohomology annihilators appear through the notion of p-standard system of parameters. For a local ring, we prove an equivalence of the existence of Macaulayfications; the existence of a p-standard system of parameters; being a quotient of a Cohen-Macaulay local ring; and the verification of Faltings' Annihilator theorem. For a finitely generated module which is unmixed and faithful, we prove an equivalence of the existence of an arithmetic Macaulayfication and the existence of a p-standard system of parameters; and both are proved to be equivalent to the existence of an arithmetic Macaulayfication on the ground ring. A connection between Macaulayfication and universal catenaricity is also discussed., Comment: 24 pages

International audience; A cell membrane can be considered a liquid-phase plane in which lipids and proteins theoretically are free to diffuse. Numerous reports, however, describe retarded diffusion of membrane proteins in animal cells. This anomalous diffusion results from a combination of structuring factors including protein-protein interactions, cytoskeleton corralling, and lipid organization into microdomains. In plant cells, plasma-membrane (PM) proteins have been described as relatively immobile, but the control mechanisms that structure the PM have not been studied. Here, we use fluorescence recovery after photobleaching to estimate mobility of a set of minimal PM proteins. These proteins consist only of a PM-anchoring domain fused to a fluorescent protein, but their mobilities remained limited, as is the case for many full-length proteins. Neither the cytoskeleton nor membrane microdomain structure was involved in constraining the diffusion of these proteins. The cell wall, however, was shown to have a crucial role in immobilizing PM proteins. In addition, by single-molecule fluorescence imaging we confirmed that the pattern of cellulose deposition in the cell wall affects the trajectory and speed of PM protein diffusion. Regulation of PM protein dynamics by the plant cell wall can be interpreted as a mechanism for regulating protein interactions in processes such as trafficking and signal transduction.

Aquaporins, channel proteins that facilitate water transport across the tonoplast and the plasma membrane of plant cells, have classically been used as reference markers for these two membranes. Yet, recent studies have shown that the subcellular localization of aquaporins is constantly adjusted in response to environmental stimuli. This chapter addresses the mechanisms that determine the density at the cell surface of aquaporins of the Plasma Membrane Intrinsic Protein (PIP) subclass. While pharmacological interference coupled to confocal imaging was extensively used in initial studies, single particle tracking of PIPs fused to GFP, fluorescence correlation spectroscopy (FCS), and a novel fluorescence recovery after photobleaching approach have provided unique insights into the peculiarity of PIP cellular dynamics. It was shown in particular that, while endocytosis of PIPs is predominantly clathrin-dependent under standard conditions, PIP cycling is enhanced under salt stress possibly involving a clathrin- and membrane raft-mediated endocytosis. Future research will address the genetic bases of these pathways and their possible control by the plant hormone auxin.

International audience; Plasma membrane intrinsic proteins (PIPs) are aquaporins that mediate water transport across the plant plasma membrane (PM). The present work addresses, using Arabidopsis AtPIP2;1 as a model, the mechanisms and significance of trafficking of newly synthesized PIPs from the endoplasmic reticulum (ER) to the Golgi apparatus. A functional diacidic export motif (Asp4-Val5-Glu6) was identified in the N-terminal tail of AtPIP2;1, using expression in transgenic Arabidopsis of site-directed mutants tagged with the green fluorescent protein (GFP). Confocal fluorescence imaging and a novel fluorescence recovery after photobleaching application based on the distinct diffusion of PM and intracellular AtPIP2;1-GFP forms revealed a retention in the ER of diacidic mutated forms, but with quantitative differences. Thus, the individual role of the two acidic Asp4 and Glu6 residues was established. In addition, expression in transgenic Arabidopsis of ER-retained AtPIP2;1-GFP constructs reduced the root hydraulic conductivity. Co-expression of AtPIP2;1-GFP and AtPIP1;4-mCherry constructs suggested that ER-retained AtPIP2;1-GFP may interact with other PIPs to hamper their trafficking to the PM, thereby contributing to inhibition of root cell hydraulic conductivity.

International audience; Aquaporins form a superfamily of intrinsic channel proteins in the plasma and intracellular membranes of plant cells. While a lot of research effort has substantiated the importance of plasma membrane aquaporins for the regulation of plant water homeostasis, comparably little is known about the function of intracellular aquaporins. Yet, various low-molecular-weight compounds, in addition to water, were recently shown to permeate some of these aquaporins. In this review, we examine the diversity of transport properties and localization patterns of intracellular aquaporins. The discussed profiles include, for example, water and ammonia transport across the tonoplast or CO2 transport through the chloroplast envelope. Furthermore, we try to assess to what extent the diverse aquaporin distribution patterns, in relation to the high degree of compartmentation of plant cells, can be linked to a wide range of cellular functions.

International audience; Aquaporins are channel proteins present in the plasma and intracellular membranes of plant cells, where they facilitate the transport of water and/or small neutral solutes (urea, boric acid, silicic acid) or gases (ammonia, carbon dioxide). Recent progress was made in understanding the molecular bases of aquaporin transport selectivity and gating. The present review examines how a wide range of selectivity profiles and regulation properties allows aquaporins to be integrated in numerous functions, throughout plant development, and during adaptations to variable living conditions. Although they play a central role in water relations of roots, leaves, seeds, and flowers, aquaporins have also been linked to plant mineral nutrition and carbon and nitrogen fixation.

International audience; Aquaporins facilitate the uptake of soil water and mediate the regulation of root hydraulic conductivity (Lp(r)) in response to a large variety of environmental stresses. Here, we use Arabidopsis (Arabidopsis thaliana) plants to dissect the effects of salt on both Lp(r) and aquaporin expression and investigate possible molecular and cellular mechanisms of aquaporin regulation in plant roots under stress. Treatment of plants by 100 mm NaCl was perceived as an osmotic stimulus and induced a rapid (half-time, 45 min) and significant (70%) decrease in Lp(r), which was maintained for at least 24 h. Macroarray experiments with gene-specific tags were performed to investigate the expression of all 35 genes of the Arabidopsis aquaporin family. Transcripts from 20 individual aquaporin genes, most of which encoded members of the plasma membrane intrinsic protein (PIP) and tonoplast intrinsic protein (TIP) subfamilies, were detected in nontreated roots. All PIP and TIP aquaporin transcripts with a strong expression signal showed a 60% to 75% decrease in their abundance between 2 and 4 h following exposure to salt. The use of antipeptide antibodies that cross-reacted with isoforms of specific aquaporin subclasses revealed that the abundance of PIP1s decreased by 40% as early as 30 min after salt exposure, whereas PIP2 and TIP1 homologs showed a 20% to 40% decrease in abundance after 6 h of treatment. Expression in transgenic plants of aquaporins fused to the green fluorescent protein revealed that the subcellular localization of TIP2;1 and PIP1 and PIP2 homologs was unchanged after 45 min of exposure to salt, whereas a TIP1;1-green fluorescent protein fusion was relocalized into intracellular spherical structures tentatively identified as intravacuolar invaginations. The appearance of intracellular structures containing PIP1 and PIP2 homologs was occasionally observed after 2 h of salt treatment. In conclusion, this work shows that exposure of roots to salt induces changes in aquaporin expression at multiple levels. These changes include a coordinated transcriptional down-regulation and subcellular relocalization of both PIPs and TIPs. These mechanisms may act in concert to regulate root water transport, mostly in the long term (> or =6 h).

Plants have to adjust their water balance in response to very challenging environmental conditions such as drought, salinity, and cold but also changes in light, nutrient deficiency or soil acidity. The molecular and functional characterization of aquaporins, a class of membrane proteins that facilitate water diffusion across cell membranes, has revealed the significance of their regulation in response to these environmental stimuli. The aim of this present review is to illustrate the variety of molecular and cellular mechanisms involved. These mechanisms include the control of aquaporin gene transcription and protein abundance, stimulus-induced aquaporin subcellular relocalization, and channel gating by reversible phosphorylation or by intracellular protons. The emergence of novel mechanisms of regulation by hetero-tetramer formation or through control by reactive oxygen species, and osmotic or hydrostatic pressure gradients is also discussed. These various mechanisms do not function individually and a challenge for future research will be to understand how plants respond to stresses by integrating these mechanisms in time and space, to constantly adjust the water transport and solute transport properties of their membranes. Genetic manipulation of aquaporin functions and in particular ectopic expression of deregulated aquaporins in transgenic plants provide promising strategies to address such questions.

Aquaporins facilitate the uptake of soil water and mediate the regulation of root hydraulic conductivity (Lpr) in response to a large variety of environmental stresses. Here, we use Arabidopsis (Arabidopsis thaliana) plants to dissect the effects of salt on both Lpr and aquaporin expression and investigate possible molecular and cellular mechanisms of aquaporin regulation in plant roots under stress. Treatment of plants by 100 mm NaCl was perceived as an osmotic stimulus and induced a rapid (half-time, 45 min) and significant (70%) decrease in Lpr, which was maintained for at least 24 h. Macroarray experiments with gene-specific tags were performed to investigate the expression of all 35 genes of the Arabidopsis aquaporin family. Transcripts from 20 individual aquaporin genes, most of which encoded members of the plasma membrane intrinsic protein (PIP) and tonoplast intrinsic protein (TIP) subfamilies, were detected in nontreated roots. All PIP and TIP aquaporin transcripts with a strong expression signal showed a 60% to 75% decrease in their abundance between 2 and 4 h following exposure to salt. The use of antipeptide antibodies that cross-reacted with isoforms of specific aquaporin subclasses revealed that the abundance of PIP1s decreased by 40% as early as 30 min after salt exposure, whereas PIP2 and TIP1 homologs showed a 20% to 40% decrease in abundance after 6 h of treatment. Expression in transgenic plants of aquaporins fused to the green fluorescent protein revealed that the subcellular localization of TIP2;1 and PIP1 and PIP2 homologs was unchanged after 45 min of exposure to salt, whereas a TIP1;1-green fluorescent protein fusion was relocalized into intracellular spherical structures tentatively identified as intravacuolar invaginations. The appearance of intracellular structures containing PIP1 and PIP2 homologs was occasionally observed after 2 h of salt treatment. In conclusion, this work shows that exposure of roots to salt induces changes in aquaporin expression at multiple levels. These changes include a coordinated transcriptional down-regulation and subcellular relocalization of both PIPs and TIPs. These mechanisms may act in concert to regulate root water transport, mostly in the long term (≥6 h).

56 ref.; International audience; The Arabidopsis genome contains many sequences annotated as encoding H+-coupled cotransporters. Amongthose are the members of the cation:proton antiporter-2 (CPA2) family (or CHX family), predicted to encodeNa+,K+/H+ antiporters. AtCHX17, a member of the CPA2 family, was selected for expression studies, andphenotypic analysis of knockout mutants was performed. AtCHX17 expression was only detected in roots. Thegene was strongly induced by salt stress, potassium starvation, abscisic acid (ABA) and external acidic pH.Using the b-glucuronidase reporter gene strategy and in situ RT-PCR experiments, we have found thatAtCHX17 was expressed preferentially in epidermal and cortical cells of the mature root zones. Knockoutmutants accumulated less Kþ in roots in response to salt stress and potassium starvation compared with thewild type. These data support the hypothesis that AtCHX17 is involved in Kþ acquisition and homeostasis

Flooding of soils results in acute oxygen deprivation (anoxia) of plant roots during winter in temperate latitudes, or after irrigation1, and is a major problem for agriculture. One early response of plants to anoxia and other environmental stresses is downregulation of water uptake due to inhibition of the water permeability (hydraulic conductivity) of roots (Lpr)2,3,4,5. Root water uptake is mediated largely by water channel proteins (aquaporins) of the plasma membrane intrinsic protein (PIP) subgroup6,7,8. These aquaporins may mediate stress-induced inhibition of Lpr2,4,9 but the mechanisms involved are unknown. Here we delineate the whole-root and cell bases for inhibition of water uptake by anoxia and link them to cytosol acidosis. We also uncover a molecular mechanism for aquaporin gating by cytosolic pH. Because it is conserved in all PIPs, this mechanism provides a basis for explaining the inhibition of Lpr by anoxia and possibly other stresses. More generally, our work opens new routes to explore pH-dependent cell signalling processes leading to regulation of water transport in plant tissues or in animal epithelia10.

Background The plant nuclear pore complex has strongly attracted the attention of the scientific community during the past few years, in particular because of its involvement in hormonal and pathogen/symbiotic signalling. In Arabidopsis thaliana, more than 30 nucleoporins have been identified, but only a few of them have been characterized. Among these, AtNUP160, AtNUP96, AtNUP58, and AtTPR have been reported to modulate auxin signalling, since corresponding mutants are suppressors of the auxin resistance conferred by the axr1 (auxin-resistant) mutation. The present work is focused on AtNUP62, which is essential for embryo and plant development. This protein is one of the three nucleoporins (with AtNUP54 and AtNUP58) of the central channel of the nuclear pore complex. Results AtNUP62 promoter activity was detected in many organs, and particularly in the embryo sac, young germinating seedlings and at the adult stage in stipules of cauline leaves. The atnup62-1 mutant, harbouring a T-DNA insertion in intron 5, was identified as a knock-down mutant. It displayed developmental phenotypes that suggested defects in auxin transport or responsiveness. Atnup62 mutant plantlets were found to be hypersensitive to auxin, at the cotyledon and root levels. The phenotype of the AtNUP62-GFP overexpressing line further supported the existence of a link between AtNUP62 and auxin signalling. Furthermore, the atnup62 mutation led to an increase in the activity of the DR5 auxin-responsive promoter, and suppressed the auxin-resistant root growth and leaf serration phenotypes of the axr1 mutant. Conclusion AtNUP62 appears to be a major negative regulator of auxin signalling. Auxin hypersensitivity of the atnup62 mutant, reminding that of atnup58 (and not observed with other nucleoporin mutants), is in agreement with the reported interaction between AtNUP62 and AtNUP58 proteins, and suggests closely related functions. The effect of AtNUP62 on auxin signalling likely occurs in relation to scaffold proteins of the nuclear pore complex (AtNUP160, AtNUP96 and AtTPR). Electronic supplementary material The online version of this article (doi:10.1186/s12870-015-0695-y) contains supplementary material, which is available to authorized users.