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Authors: Jianwu Li, Shuaibing Yao, Sang-Chul Kim and Xuemin Wang.
Molecular Plant (2024)
Abstract: "Lipid phosphorylation by diacylglycerol kinase (DGK) that produces phosphatidic acid (PA) plays important roles in various biological processes, including stress responses, but the mechanism of action remains elusive. Here we show that DGK5 and its lipid product PA suppress ABA biosynthesis by interacting with ABA DEFICIENT 2 (ABA2), a key ABA biosynthesis enzyme, to negatively modulate plant response to abiotic stress tested in Arabidopsis thaliana. Loss of DGK5 function rendered plants less damaged, whereas its overexpression (OE) enhanced plant damage to water and salt stress, compared to wild type (WT). The dgk5 mutant plants exhibited decreased total cellular and nuclear levels of PA with increased levels of diacylglycerol (DAG), whereas DGK5-OE displayed the opposite effect. DGK5 and PA bound to the ABA-synthesizing enzyme ABA DEFICIENT 2 (ABA2) and suppressed its enzymatic activity. The dgk5 mutant plants exhibited increased levels of ABA, while DGK5-OE plants showed reduced ABA levels. In addition, both DGK5 and ABA2 are detected in and outside nuclei, and the loss of DGK5 decreased the nuclear association of ABA2. DGK5 activity and PA promoted ABA2’s nuclear association. Taken together, those results show that DGK5 and PA interact with ABA2 and suppress ABA production by both inhibiting its enzymatic activity and promoting nuclear sequestration of ABA2, revealing a mechanism by which DGK5 and PA regulate plant stress responses."
Author: Hongtao Liu.
Curent Biology (2023)
Summary: Blue light triggers stomatal opening through the phototropin-mediated pathway. A new study shows that light-induced stomatal opening is negatively regulated by three closely related plastidial phospholipases and their downstream oxylipin product.
Excerpts: "In this issue of Current Biology, Chang et al. show that the stomatal response to blue light is negatively regulated by 12-oxo-phytodienoic acid (OPDA), an oxylipin metabolite, and in doing so reveal a new role for chloroplast membrane metabolism in stomatal regulation"
"In the new paper by Chang et al.2, they exploited a cell-type-specific transcriptomic strategy to identify genes that exhibit differential expression patterns in the leaf’s epidermis during the pre- to post-dawn transition, when stomata open in response to blue light. RNA-Seq analysis revealed that the expression of three paralogous genes, namely PLIP1, PLIP2, and PLIP3, which encode plastidial lipid-degrading enzymes, was enhanced in guard cells upon illumination (Figure 1). Genetic defects in these genes caused faster stomatal opening, indicating the involvement of these plastidial lipases in the negative regulation of stomatal aperture (Figure 1)."
Authors: Qianru Jia, Yang Bai, Hui Xu, Qingyun Liu, Wenyan Li, Teng Li, Feng Lin, Like Shen, Wei Xuan, Wenhua Zhang and Qun Zhang.
PNAS (2022)
Significance: Lysophosphatidic acid (LPA) is an anionic bioactive phospholipid. In this study, we explored whether and how LPA signaling impacts plant growth and development and discovered that LPA-controlled membrane properties modulate the PIN-FORMED1 (PIN1) auxin efflux transporter, which is linked to the plasma membrane and polar auxin transport in plants. Our findings reveal a fundamental role of lipid metabolism in controlling embryonic and postembryonic development, as well as mechanistically interconnecting membrane LPA and PIN1 in the fine-tuned regulation of auxin signaling.
Abstract: "Membrane properties are emerging as important cues for the spatiotemporal regulation of hormone signaling. Lysophosphatidic acid (LPA) evokes multiple biological responses by activating G protein–coupled receptors in mammals. In this study, we demonstrated that LPA derived from the mitochondrial glycerol-3-phosphate acyltransferases GPAT1 and GPAT2 is a critical lipid-based cue for auxin-controlled embryogenesis and plant growth in Arabidopsis thaliana. LPA levels decreased, and the polarity of the auxin efflux carrier PIN-FORMED1 (PIN1) at the plasma membrane (PM) was defective in the gpat1 gpat2 mutant. As a consequence of distribution defects, instructive auxin gradients and embryonic and postembryonic development are severely compromised. Further cellular and genetic analyses revealed that LPA binds directly to PIN1, facilitating the vesicular trafficking of PIN1 and polar auxin transport. Our data support a model in which LPA provides a lipid landmark that specifies membrane identity and cell polarity, revealing an unrecognized aspect of phospholipid patterns connecting hormone signaling with development."
Authors: Nargis Parvin Laha, Ricardo F. H. Giehl, Esther Riemer, Danye Qiu, Naga Jyothi Pullagurla, Robin Schneider, Yashika Walia Dhir, Ranjana Yadav, Yeshambel Emewodih Mihiret, Philipp Gaugler, Verena Gaugler, Haibin Mao, Ning Zheng, Nicolaus von Wirén, Adolfo Saiardi, Saikat Bhattacharjee, Henning J. Jessen, Debabrata Laha and Gabriel Schaaf.
Plant Physiology (2022)
Abstract: "The combinatorial phosphorylation of myo-inositol results in the generation of different inositol phosphates (InsPs), of which phytic acid (InsP6) is the most abundant species in eukaryotes. InsP6 is also an important precursor of the higher phosphorylated inositol pyrophosphates (PP-InsPs), such as InsP7 and InsP8, which are characterized by a diphosphate moiety and are also ubiquitously found in eukaryotic cells. While PP-InsPs regulate various cellular processes in animals and yeast, their biosynthesis and functions in plants has remained largely elusive because plant genomes do not encode canonical InsP6 kinases. Recent work has shown that Arabidopsis (Arabidopsis thaliana) INOSITOL (1,3,4) TRIPHOSPHATE 5/6 KINASE1 (ITPK1) and ITPK2 display in vitro InsP6 kinase activity and that, in planta, ITPK1 stimulates 5-InsP7 and InsP8 synthesis and regulates phosphate starvation responses. Here we report a critical role of ITPK1 in auxin-related processes that is independent of the ITPK1-controlled regulation of phosphate starvation responses. Those processes include primary root elongation, root hair development, leaf venation, thermomorphogenic and gravitropic responses, and sensitivity to exogenously applied auxin. We found that the recombinant auxin receptor complex, consisting of the F-Box protein TRANSPORT INHIBITOR RESPONSE1 (TIR1), ARABIDOPSIS SKP1 HOMOLOGUE 1 (ASK1) and the transcriptional repressor INDOLE-3-ACETIC ACID INDUCIBLE 7 (IAA7), binds to anionic inositol polyphosphates with high affinity. We further identified a physical interaction between ITPK1 and TIR1, suggesting a localized production of 5-InsP7, or another ITPK1-dependent InsP/PP-InsP isomer, to activate the auxin receptor complex. Finally, we demonstrate that ITPK1 and ITPK2 function redundantly to control auxin responses, as deduced from the auxin-insensitive phenotypes of itpk1 itpk2 double mutant plants. Our findings expand the mechanistic understanding of auxin perception and suggest that distinct inositol polyphosphates generated near auxin receptors help to fine-tune auxin sensitivity in plants."
Authors: Anastasiia Starodubtseva, Tetiana Kalachova, Katarzyna Retzer, Adriana Jelínková, Petre Dobrev, Jozef Lacek, Romana Pospíchalová, Jindřiška Angelini, Anne Guivarc’h, Stéphanie Pateyron, Ludivine Soubigou-Taconnat, Lenka Burketová and Eric Ruelland.
Scientific Reports (2022)
Abstract: "Phosphatidylinositol 4-kinases (PI4Ks) are the first enzymes that commit phosphatidylinositol into the phosphoinositide pathway. Here, we show that Arabidopsis thaliana seedlings deficient in PI4Kβ1 and β2 have several developmental defects including shorter roots and unfinished cytokinesis. The pi4kβ1β2 double mutant was insensitive to exogenous auxin concerning inhibition of root length and cell elongation; it also responded more slowly to gravistimulation. The pi4kβ1β2 root transcriptome displayed some similarities to a wild type plant response to auxin. Yet, not all the genes displayed such a constitutive auxin-like response. Besides, most assessed genes did not respond to exogenous auxin. This is consistent with data with the transcriptional reporter DR5-GUS. The content of bioactive auxin in the pi4kβ1β2 roots was similar to that in wild-type ones. Yet, an enhanced auxin-conjugating activity was detected and the auxin level reporter DII-VENUS did not respond to exogenous auxin in pi4kβ1β2 mutant. The mutant exhibited altered subcellular trafficking behavior including the trapping of PIN-FORMED 2 protein in rapidly moving vesicles. Bigger and less fragmented vacuoles were observed in pi4kβ1β2 roots when compared to the wild type. Furthermore, the actin filament web of the pi4kβ1β2 double mutant was less dense than in wild-type seedling roots, and less prone to rebuilding after treatment with latrunculin B. A mechanistic model is proposed in which an altered PI4K activity leads to actin filament disorganization, changes in vesicle trafficking, and altered auxin homeostasis and response resulting in a pleiotropic root phenotypes."
Authors: Sheng Zheng, Min Su, Lu Wang, Tengguo Zhang, Juan Wang, Huichun Xie, Xuexia Wu, Syed Inzimam Ul Haq and Quan-Sheng Qiu.
Journal of Plant Physiology (2021)
Abstract: "Cold stress is one of the harsh environmental stresses that adversely affect plant growth and crop yields in the Qinghai-Tibet Plateau. However, plants have evolved mechanisms to overcome the impact of cold stress. Progress has been made in understanding how plants perceive and transduce low-temperature signals to tolerate cold stress. Small signaling molecules are crucial for cellular signal transduction by initiating the downstream signaling cascade that helps plants to respond to cold stress. These small signaling molecules include calcium, reactive oxygen species, nitric oxide, hydrogen sulfide, cyclic guanosine monophosphate, phosphatidic acid, and sphingolipids. The small signaling molecules are involved in many aspects of cellular and physiological functions, such as inducing gene expression and activating hormone signaling, resulting in upregulation of the antioxidant enzyme activities, protestantesimo accumulation, malondialdehyde reduction, and photosynthesis improvement. We summarize our current understanding of the roles of the small signaling molecules in cold stress in plants, and highlight their crosstalk in cold signaling transduction. These discoveries help us understand how the plateau plants adapt to the severe alpine environment as well as to develop new crops tolerating cold stress in the Qinghai-Tibet Plateau.
Authors: Hendry Susila, Snježana Jurić, Lu Liu, Katarzyna Gawarecka, Kyung Sook Chung, Suhyun Jin, Soo-Jin Kim, Zeeshan Nasim, Geummin Youn, Mi Chung Suh, Hao Yu and Ji Hoon Ahn.
Science (2021)
Editor's view: Linking flowering to ambient temperature In the small mustard plant Arabidopsis, the florigen FLOWERING LOCUS T (FT) mobilizes to initiate flowering at the shoot apical meristem. Susila et al. now show that FT, which is produced in leaf cells, can be held in reserve if ambient temperatures are not favorable (see the Perspective by Jaillais and Parcy). At low temperatures, FT binds a membrane phosopholipid and is thus restricted in mobility. At higher temperatures, such binding is less favored, and FT is released to mobilize into the shoot apical meristem to drive flowering. Thus, temperature-sensitive lipid binding helps the plant time flowering with favorable ambient temperatures.
Abstract: "Plants respond to temperature changes by modulating florigen activity to optimize the timing of flowering. We show that the Arabidopsis thaliana mobile florigen FLOWERING LOCUS T (FT) interacts with the negatively charged phospholipid phosphatidylglycerol (PG) at cellular membranes and binds the lipid bilayer. Perturbing PG biosynthesis in phloem companion cells leads to temperature-insensitive early flowering. Low temperatures facilitate FT sequestration in the cellular membrane of the companion cell, thus reducing soluble FT levels and delaying flowering. A mutant in PHOSPHATIDYLGLYCEROLPHOSPHATE SYNTHASE 1 accumulates more soluble FT at lower temperatures and exhibits reduced temperature sensitivity. Thus, cellular membranes sequester FT through their ability to bind the phospholipid PG, and this sequestration modulates the plant’s response to temperature changes."
Authors: Yoko Ito, Nicolas Esnay, Matthieu Pierre Platre, Valérie Wattelet-Boyer, Lise C. Noack, Louise Fougère, Wilhelm Menzel, Stéphane Claverol, Laetitia Fouillen, Patrick Moreau, Yvon Jaillais and Yohann Boutté.
Nature Communications (2021)
Editor's view: Lipid composition impacts the function of cellular membranes. Here the authors show that a reduction in sphingolipid acyl-chain length promotes phosphoinositide consumption by phospholipase C at the Arabidopsis trans-Golgi network which in turn regulates sorting of the auxin efflux carrier PIN2.
Abstract: "The lipid composition of organelles acts as a landmark to define membrane identity and specify subcellular function. Phosphoinositides are anionic lipids acting in protein sorting and trafficking at the trans-Golgi network (TGN). In animal cells, sphingolipids control the turnover of phosphoinositides through lipid exchange mechanisms at endoplasmic reticulum/TGN contact sites. In this study, we discover a mechanism for how sphingolipids mediate phosphoinositide homeostasis at the TGN in plant cells. Using multiple approaches, we show that a reduction of the acyl-chain length of sphingolipids results in an increased level of phosphatidylinositol-4-phosphate (PtdIns(4)P or PI4P) at the TGN but not of other lipids usually coupled to PI4P during exchange mechanisms. We show that sphingolipids mediate Phospholipase C (PLC)-driven consumption of PI4P at the TGN rather than local PI4P synthesis and that this mechanism is involved in the polar sorting of the auxin efflux carrier PIN2 at the TGN. Together, our data identify a mode of action of sphingolipids in lipid interplay at the TGN during protein sorting."
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Authors: Kwang-Ho Maeng, Hyodong Lee and Hyung-Taeg Cho.
PNAS (2023)
Significance: Phosphatidylinositol kinases are instrumental in endomembrane cargo trafficking by altering local membrane-lipid properties, and PIN-FORMED (PIN) auxin efflux transporters exhibit dynamic intracellular trafficking patterns modulated by the phosphorylation of their hydrophilic loop (HL) domain. Yet, the mechanisms by which phosphatidylinositol kinase establishes the trafficking pathway and selectivity of cargo and how PIN-HL phosphorylation influences PIN trafficking remained enigmatic. This study unveils that FAB1C, a phosphatidylinositol-3-phosphate 5-kinase in Arabidopsis, interfaces directly with PIN-HL, orchestrating PIN's vacuolar trafficking in a PIN-HL phosphorylation-dependent manner. These findings offer a leap forward in deciphering the interplay between membrane-lipid modifiers and cargo selection for endomembrane trafficking and the role of PIN phosphorylation in trafficking, enhancing our understanding of complex eukaryotic cellular processes.
Abstract: "PIN-FORMEDs (PINs) are auxin efflux carriers that asymmetrically target the plasma membrane (PM) and are critical for forming local auxin gradients and auxin responses. While the cytoplasmic hydrophilic loop domain of PIN (PIN-HL) is known to include some molecular cues (e.g., phosphorylation) for the modulation of PIN’s intracellular trafficking and activity, the complexity of auxin responses suggests that additional regulatory modules may operate in the PIN-HL domain. Here, we have identified and characterized a PIN-HL-interacting protein (PIP) called FORMATION OF APLOID AND BINUCLEATE CELL 1C (FAB1C), a phosphatidylinositol-3-phosphate 5-kinase, which modulates PIN's lytic trafficking. FAB1C directly interacts with PIN-HL and is required for the polarity establishment and vacuolar trafficking of PINs. Unphosphorylated forms of PIN2 interact more readily with FAB1C and are more susceptible to vacuolar lytic trafficking compared to phosphorylated forms. FAB1C also affected lateral root formation by modulating the abundance of periclinally localized PIN1 and auxin maximum in the growing lateral root primordium. These findings suggest that a membrane-lipid modifier can target the cargo-including vesicle by directly interacting with the cargo and modulate its trafficking depending on the cargo’s phosphorylation status."
Authors: Qian Wang, A. Cecilia Aliaga Fandino, Moritz Graeff, Thomas A. DeFalco, Cyril Zipfel and Christian S. Hardtke.
Nature Communications (2023)
One-sentence summary: In this paper the authors demonstrate that auxin efflux in the phloem vascular tissue of plants is determined by antagonism between CLE peptide signaling pathways and phosphoinositide kinases.
Abstract: "Auxin efflux through plasma-membrane-integral PIN-FORMED (PIN) carriers is essential for plant tissue organization and tightly regulated. For instance, a molecular rheostat critically controls PIN-mediated auxin transport in developing protophloem sieve elements of Arabidopsis roots. Plasma-membrane-association of the rheostat proteins, BREVIS RADIX (BRX) and PROTEIN KINASE ASSOCIATED WITH BRX (PAX), is reinforced by interaction with PHOSPHATIDYLINOSITOL-4-PHOSPHATE-5-KINASE (PIP5K). Genetic evidence suggests that BRX dampens autocrine signaling of CLAVATA3/EMBRYO SURROUNDING REGION-RELATED 45 (CLE45) peptide via its receptor BARELY ANY MERISTEM 3 (BAM3). How excess CLE45-BAM3 signaling interferes with protophloem development and whether it does so directly or indirectly remains unclear. Here we show that rheostat polarity is independent of PIN polarity, but interdependent with PIP5K. Catalytically inactive PIP5K confers rheostat polarity without reinforcing its localization, revealing a possible PIP5K scaffolding function. Moreover, PIP5K and PAX cooperatively control local PIN abundance. We further find that CLE45-BAM3 signaling branches via RLCK-VII/PBS1-LIKE (PBL) cytoplasmic kinases to destabilize rheostat localization. Our data thus reveal antagonism between CLE45-BAM3-PBL signaling and PIP5K that converges on auxin efflux regulation through dynamic control of PAX polarity. Because second-site bam3 mutation suppresses root as well as shoot phenotypes of pip5k mutants, CLE peptide signaling likely modulates phosphoinositide-dependent processes in various developmental contexts."
Authors: Teng Li, Xingkai Xiao, Qingyun Liu, Wenyan Li, Li Li, Wenhua Zhang, Teun Munnik, Xuemin Wang and Qun Zhang.
Plant Communications (2022)
Abstract: "Membrane fluidity, permeability, and surface charges are controlled by phospholipid metabolism and transport. Despite the importance of phosphatidic acid (PA) as a bioactive molecule, the mechanical properties of PA translocation and subcellular accumulation are unknown. Here, we used a mobilizable, highly responsive genetically encoded fluorescent indicator, GFP-N160RbohD, for monitoring PA dynamics in living cells. The majority of GFP-N160RbohD accumulated at the plasma membrane and sensitively responded to changes in PA levels. Cellular, pharmacological, and genetic analyses illustrated that both salinity and abscisic acid rapidly enhanced GFP-N160RbohD fluorescence at the plasma membrane, which mainly depended on the hydrolysis of phospholipase D (PLD). In contrast, heat stress induces nuclear translocation of PA indicated by GFP-N160RbohD through a process that requires diacylglycerol kinase activity, as well as secretory and endocytic trafficking. Strikingly, we showed that gravity triggers asymmetric PA distribution at the root apex, a response that is suppressed by PLDζ2 knockout. The broad utility of the PA sensor will expand our mechanistic understanding of numerous lipid-associated physiological and cell biological processes, and facilitate screening for protein candidates that affect the synthesis, transport, and metabolism of PA.
Authors: Claudia von der Mark, Tiago M. D. Cruz, Noel Blanco-Touriñan and Antia Rodriguez-Villalon.
New Phytologist (2022)
Abstract: "Efficient root-to-shoot delivery of water and nutrients in plants relies on the correct differentiation of xylem cells into hollow elements. While auxin is integral to the formation of xylem cells, it remains poorly characterized how each subcellular pool of this hormone regulates this process. Combining genetic and cell biological approaches, we investigated the bipartite activity of nucleoplasmic vs plasma membrane-associated phosphatidylinositol 4-phosphate kinases PIP5K1 and its homologue PIP5K2 in Arabidopsis thaliana roots and uncovered a novel mechanism by which phosphoinositides integrate distinct aspects of the auxin signaling cascade and, in turn, regulate the onset of xylem differentiation. The appearance of undifferentiated cells in protoxylem strands of pip5k1 pip5k2 is phenomimicked in auxin transport and perception mutants and can be partially restored by the nuclear residence of PIP5K1. Instead, exclusion of PIP5K1 from the nucleus hinders the auxin-mediated induction of the xylem master regulator VASCULAR RELATED NAC DOMAIN (VND) 7. A xylem-specific increase of auxin levels abolishes pip5k1 pip5k2 vascular defects, indicating that the establishment of auxin maxima is required to activate VND7-mediated xylem differentiation. Our results describe a new mechanism by which distinct subcellular pools of phosphoinositides integrate auxin transport and perception to initiate xylem differentiation in a spatio-temporal manner."
Authors: Leia Colin and Olivier Hamant.
Comptes Rendus. Biologies (2021)
Abstract: "The plasma membrane is a physical boundary made of amphiphilic lipid molecules, proteins and carbohydrates extensions. Its role in mechanotransduction generates increasing attention in animal systems, where membrane tension is mainly induced by cortical actomyosin. In plant cells, cortical tension is of osmotic origin. Yet, because the plasma membrane in plant cells has comparable physical properties, findings from animal systems likely apply to plant cells too. Recent results suggest that this is indeed the case, with a role of membrane tension in vesicle trafficking, mechanosensitive channel opening or cytoskeleton organization in plant cells. Prospects for the plant science community are at least three fold: (i) to develop and use probes to monitor membrane tension in tissues, in parallel with other biochemical probes, with implications for protein activity and nanodomain clustering, (ii) to develop single cell approaches to decipher the mechanisms operating at the plant cell cortex at high spatio-temporal resolution, and (iii) to revisit the role of membrane composition at cell and tissue scale, by considering the physical implications of phospholipid properties and interactions in mechanotransduction."
Authors: Yvon Jaillais and François Parcy
Science (2021)
Excerpts: "Although conserved throughout flowering plants, the function of FT lipid-binding capacity has remained enigmatic. On page 1137 of this issue, Susila et al. (3) show that FT binds to the anionic phospholipid phosphatidylglycerol, which sequesters FT in membrane compartments of phloem cells at low temperature, thereby delaying flowering in cold conditions. Thus, a temperature-dependent regulation of FT translocation by a membrane phospholipid tunes the plant response to ambient temperature. Susila et al. found that FT binds to the anionic phospholipid phosphatidylglycerol in vitro and in phloem cells in vivo."
"Susila et al. found that in A. thaliana protoplasts (plant cells without a cell wall), FT associates with various membranes that contain phosphatidylglycerol: the plasma membrane, Golgi apparatus, trans-Golgi network, endoplasmic reticulum, and chloroplast envelope. Low temperature (i.e., a long day at 16°C) induced the interaction between FT and cellular membranes in a phosphatidylglycerol-dependent manner."
"Low temperature promotes the phosphatidylglycerol-dependent retention of FT in cellular membranes of companion cells, which delays flowering by reducing FT movement toward the sieve elements and thus the shoot meristem. In phosphatidylglycerol biosynthetic mutants, this temperature-dependent retention is reduced, leading to an early flowering phenotype and temperature insensitivity. During long days at 23°C, FT is not sequestered within companion cell membranes and moves into phloem sieve elements to reach the shoot apical meristem and accelerate flowering."
Authors: Huasheng Cao, Rong Gong, Shu Yuan, Yuan Su, Weixin Lv, Yimeng Zhou, Qingqing Zhang, Xianjun Deng, Pan Tong, Shihu Liang, Xuemin Wang and Yueyun Hong.
EMBO reports (2021)
Editor's view: Phospholipase Dα6 and the lipid phosphatidic acid (PA) mediate gibberellin (GA) signalling in rice. PLDα6 and PA promote the nuclear localization of the gibberellin receptor GID1 and the degradation of the DELLA protein SLENDER RICE1 (SLR1), enhancing GA signaling.
Abstract: "Phospholipase D (PLD) hydrolyzes membrane lipids to produce phosphatidic acid (PA), a lipid mediator involved in various cellular and physiological processes. Here, we show that PLDα6 and PA regulate the distribution of GIBBERELLIN (GA)-INSENSITIVE DWARF1 (GID1), a soluble gibberellin receptor in rice. PLDα6-knockout (KO) plants display less sensitivity to GA than WT, and PA restores the mutant to a normal GA response. PA binds to GID1, as documented by liposome binding, fat immunoblotting, and surface plasmon resonance. Arginines 79 and 82 of GID1 are two key amino acid residues required for PA binding and also for GID1’s nuclear localization. The loss of PLDα6 impedes GA-induced nuclear localization of GID1. In addition, PLDα6-KO plants attenuated GA-induced degradation of the DELLA protein SLENDER RICE1 (SLR1). These data suggest that PLDα6 and PA positively mediate GA signaling in rice via PA binding to GID1 and promotion of its nuclear translocation."
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