scholarly journals TRANVIA (TVA) facilitates cellulose synthase trafficking and delivery to the plasma membrane

2021 ◽  
Vol 118 (30) ◽  
pp. e2021790118
Author(s):  
Tamara Vellosillo ◽  
José R. Dinneny ◽  
Chris R. Somerville ◽  
David W. Ehrhardt
Keyword(s):  
Plasma Membrane ◽  
Molecular Mechanisms ◽  
Cellulose Synthase ◽  
Specific Protein ◽  
Primary Cell Wall ◽  
Cellulose Synthesis ◽  
Cellulose Content ◽  
Enhanced Sensitivity ◽  
Intracellular Compartments ◽  
Secretory System

Cellulose is synthesized at the plasma membrane by cellulose synthase (CESA) complexes (CSCs), which are assembled in the Golgi and secreted to the plasma membrane through the trans-Golgi network (TGN) compartment. However, the molecular mechanisms that guide CSCs through the secretory system and deliver them to the plasma membrane are poorly understood. Here, we identified an uncharacterized gene, TRANVIA (TVA), that is transcriptionally coregulated with the CESA genes required for primary cell wall synthesis. The tva mutant exhibits enhanced sensitivity to cellulose synthesis inhibitors; reduced cellulose content; and defective dynamics, density, and secretion of CSCs to the plasma membrane as compared to wild type. TVA is a plant-specific protein of unknown function that is detected in at least two different intracellular compartments: organelles labeled by markers for the TGN and smaller compartments that deliver CSCs to the plasma membrane. Together, our data suggest that TVA promotes trafficking of CSCs to the plasma membrane by facilitating exit from the TGN and/or interaction of CSC secretory vesicles with the plasma membrane.

scholarly journals CSI1, PATROL1, and exocyst complex cooperate in delivery of cellulose synthase complexes to the plasma membrane

2018 ◽  
Vol 115 (15) ◽  
pp. E3578-E3587 ◽  
Author(s):  
Xiaoyu Zhu ◽  
Shundai Li ◽  
Songqin Pan ◽  
Xiaoran Xin ◽  
Ying Gu
Keyword(s):  
Plasma Membrane ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
De Novo ◽  
Cellulose Synthase ◽  
Specific Protein ◽  
Cellulose Synthesis ◽  
Docking Site ◽  
Multiple Components ◽  
Exocyst Complex

Cellulose synthesis occurs exclusively at the plasma membrane by cellulose synthase complexes (CSCs). Therefore, delivery of CSCs to discrete sites at the plasma membrane is critical for cellulose synthesis. Despite their significance, the delivery of CSCs is poorly understood. Here we used proteomics approaches, functional genetics, and live cell imaging to show that the de novo secretion of CSCs is mediated by cooperation among cellulose synthase interactive 1 (CSI1), the plant-specific protein PATROL1, and exocyst complex in Arabidopsis thaliana. We propose that CSI1 plays a role in marking the docking site, which allows CSCs-containing vesicles access to the plasma membrane through its interaction with microtubules. PATROL1 assists in exocytosis by its interaction with multiple components, including CSI1, CSCs, and exocyst subunits. Both PATROL1 and the exocyst complex determine the rate of delivery of CSCs to the plasma membrane. By monitoring the exocyst complex, PATROL1, CSI1, and CSCs dynamics in real time, we present a timeline of events for exocytosis of CSCs. Our findings provide unique insights into the evolution of exocytosis in eukaryotes.

scholarly journals Disruption of Very-Long-Chain-Fatty Acid Synthesis Has an Impact on the Dynamics of Cellulose Synthase in Arabidopsis thaliana

Plants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1599
Author(s):  
Xiaoyu Zhu ◽  
Frédérique Tellier ◽  
Ying Gu ◽  
Shundai Li
Keyword(s):  
Fatty Acid ◽  
Cell Biology ◽  
Higher Plants ◽  
Threshold Level ◽  
Cellulose Synthase ◽  
Chain Fatty Acid ◽  
Cellulose Synthesis ◽  
Cellulose Content ◽  
Long Chain Fatty Acid ◽  
Long Chain

In higher plants, cellulose is synthesized by membrane-spanning large protein complexes named cellulose synthase complexes (CSCs). In this study, the Arabidopsis PASTICCINO2 (PAS2) was identified as an interacting partner of cellulose synthases. PAS2 was previously characterized as the plant 3-hydroxy-acyl-CoA dehydratase, an ER membrane-localized dehydratase that is essential for very-long-chain-fatty acid (VLCFA) elongation. The pas2-1 mutants show defective cell elongation and reduction in cellulose content in both etiolated hypocotyls and light-grown roots. Although disruption of VLCFA synthesis by a genetic alteration had a reduction in VLCFA in both etiolated hypocotyls and light-grown roots, it had a differential effect on cellulose content in the two systems, suggesting the threshold level of VLCFA for efficient cellulose synthesis may be different in the two biological systems. pas2-1 had a reduction in both CSC delivery rate and CSC velocity at the PM in etiolated hypocotyls. Interestingly, Golgi but not post-Golgi endomembrane structures exhibited a severe defect in motility. Experiments using pharmacological perturbation of VLCFA content in etiolated hypocotyls strongly indicate a novel function of PAS2 in the regulation of CSC and Golgi motility. Through a combination of genetic, biochemical and cell biology studies, our study demonstrated that PAS2 as a multifunction protein has an important role in the regulation of cellulose biosynthesis in Arabidopsis hypocotyl.

scholarly journals Exogenous Application of Low-Concentration Sugar Enhances Brassinosteroid Signaling for Skotomorphogenesis by Promoting BIN2 Degradation

2021 ◽  
Vol 22 (24) ◽  
pp. 13588
Author(s):  
Huachun Sheng ◽  
Shuangxi Zhang ◽  
Yanping Wei ◽  
Shaolin Chen
Keyword(s):  
Plant Growth ◽  
Molecular Mechanisms ◽  
Cellulose Synthesis ◽  
Cellulose Content ◽  
Growth Responses ◽  
Phenotypic Analysis ◽  
Triple Mutant ◽  
Low Concentration ◽  
Etiolated Seedlings ◽  
Dependent Growth

In plants, seedling growth is subtly controlled by multiple environmental factors and endogenous phytohormones. The cross-talk between sugars and brassinosteroid (BR) signaling is known to regulate plant growth; however, the molecular mechanisms that coordinate hormone-dependent growth responses with exogenous sucrose in plants are incompletely understood. Skotomorphogenesis is a plant growth stage with rapid elongation of the hypocotyls. In the present study, we found that low-concentration sugars could improve skotomorphogenesis in a manner dependent on BR biosynthesis and TOR activation. However, accumulation of BZR1 in bzr1-1D mutant plants partially rescued the defects of skotomorphogenesis induced by the TOR inhibitor AZD, and these etiolated seedlings displayed a normal phenotype like that of wild-type seedlings in response to both sucrose and non-sucrose treatments, thereby indicating that accumulated BZR1 sustained, at least partially, the sucrose-promoted growth of etiolated seedlings (skotomorphogenesis). Moreover, genetic evidence based on a phenotypic analysis of bin2-3bil1bil2 triple-mutant and gain-of-function bin2–1 mutant plant indicated that BIN2 inactivation was conducive to skotomorphogenesis in the dark. Subsequent biochemical and molecular analyses enabled us to confirm that sucrose reduced BIN2 levels via the TOR–S6K2 pathway in etiolated seedlings. Combined with a determination of the cellulose content, our results indicated that sucrose-induced BIN2 degradation led to the accumulation of BZR1 and the enhancement of cellulose synthesis, thereby promoting skotomorphogenesis, and that BIN2 is the converging node that integrates sugar and BR signaling.

scholarly journals BRASSINOSTEROID INSENSITIVE2 negatively regulates cellulose synthesis in Arabidopsis by phosphorylating cellulose synthase 1

2017 ◽  
Vol 114 (13) ◽  
pp. 3533-3538 ◽  
Author(s):  
Clara Sánchez-Rodríguez ◽  
KassaDee Ketelaar ◽  
Rene Schneider ◽  
Jose A. Villalobos ◽  
Chris R. Somerville ◽  
...  
Keyword(s):  
Phosphorylation Site ◽  
Point Mutations ◽  
Cellulose Synthase ◽  
Negative Regulator ◽  
Primary Cell Wall ◽  
Cellulose Synthesis ◽  
Cellulose Biosynthesis ◽  
Plant Growth And Development ◽  
Cellulose Synthase Complex ◽  
A Subunit

The deposition of cellulose is a defining aspect of plant growth and development, but regulation of this process is poorly understood. Here, we demonstrate that the protein kinase BRASSINOSTEROID INSENSITIVE2 (BIN2), a key negative regulator of brassinosteroid (BR) signaling, can phosphorylate Arabidopsis cellulose synthase A1 (CESA1), a subunit of the primary cell wall cellulose synthase complex, and thereby negatively regulate cellulose biosynthesis. Accordingly, point mutations of the BIN2-mediated CESA1 phosphorylation site abolished BIN2-dependent regulation of cellulose synthase activity. Hence, we have uncovered a mechanism for how BR signaling can modulate cellulose synthesis in plants.

scholarly journals Expression Patterns and Gene Analysis of the Cellulose Synthase Gene Superfamily in Eucalyptus grandis

Forests ◽  
2021 ◽  
Vol 12 (9) ◽  
pp. 1254
Author(s):  
Guo Liu ◽  
Yaojian Xie ◽  
Xiuhua Shang ◽  
Zhihua Wu
Keyword(s):  
Gene Expression ◽  
Cell Wall ◽  
Expression Pattern ◽  
Expression Patterns ◽  
Cellulose Synthase ◽  
Primary Cell Wall ◽  
Regulation Mechanism ◽  
Cellulose Content ◽  
Qrt Pcr ◽  
Different Parts

Cellulose is the world’s most abundant renewable energy resource, and a variety of cellulose synthase genes are involved in the biosynthesis of cellulose. In the process of cellulose synthesis, all cellulose synthases are interrelated and act synergistically. In this study, we analyzed the contents of cellulose, hemicellulose, and lignin in the different parts and tissues of E. grandis. The results showed that the cellulose content had greater differences among three different heights. On this basis, we carried out the transcriptome-wide profiling of gene expression patterns using RNA sequencing. A total of 2066 differentially expressed genes were identified for three pairwise comparisons between three different heights, most of which were related to the programmed photosynthetic membrane and photosystem. A total of 100 transcripts of CSs (58 CesA and 42 Csl) were obtained from transcriptome libraries. The expression pattern of these genes indicated that different CS genes had a wide range of expression profiles. A phylogenetic analysis of 135 reference CS genes showed that the CSs of E. grandis were clustered into six major groups (CesA1-9, CslA, CslB/H, CslD, CslE, and CslG). Based on the weighted gene co-expression network analysis, a dual-directional regulation mechanism between Csl and CesA proteins in the cellulose biosynthesis was identified. The gene expression profile analysis, using qRT-PCR in different tissues of E. grandis, demonstrated that the CSs were highly expressed in xylem, and CesAs had a higher relative expression than Csls. The analysis of sequence similarity combined with the expression pattern indicated that the CesA1, 3, and 6 transcripts were associated with the biosynthesis of the secondary cell wall, and CesA4, 5, and 7 transcripts were more likely to associate with the biosynthesis of the primary cell wall. Finally, the qRT-PCR analysis confirmed the expression of 11 selected CSs in three different parts of E. grandis.

scholarly journals Cellulose synthase complexes display distinct dynamic behaviors during xylem transdifferentiation

2018 ◽  
Vol 115 (27) ◽  
pp. E6366-E6374 ◽  
Author(s):  
Yoichiro Watanabe ◽  
Rene Schneider ◽  
Sarah Barkwill ◽  
Eliana Gonzales-Vigil ◽  
Joseph L. Hill ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Expansion ◽  
Secondary Wall ◽  
Transition Period ◽  
Cellulose Synthase ◽  
Wall Thickening ◽  
Cellulose Synthesis ◽  
Primary Wall ◽  
Dynamic Behaviors

In plants, plasma membrane-embedded CELLULOSE SYNTHASE (CESA) enzyme complexes deposit cellulose polymers into the developing cell wall. Cellulose synthesis requires two different sets of CESA complexes that are active during cell expansion and secondary cell wall thickening, respectively. Hence, developing xylem cells, which first undergo cell expansion and subsequently deposit thick secondary walls, need to completely reorganize their CESA complexes from primary wall- to secondary wall-specific CESAs. Using live-cell imaging, we analyzed the principles underlying this remodeling. At the onset of secondary wall synthesis, the primary wall CESAs ceased to be delivered to the plasma membrane and were gradually removed from both the plasma membrane and the Golgi. For a brief transition period, both primary wall- and secondary wall-specific CESAs coexisted in banded domains of the plasma membrane where secondary wall synthesis is concentrated. During this transition, primary and secondary wall CESAs displayed discrete dynamic behaviors and sensitivities to the inhibitor isoxaben. As secondary wall-specific CESAs were delivered and inserted into the plasma membrane, the primary wall CESAs became concentrated in prevacuolar compartments and lytic vacuoles. This adjustment in localization between the two CESAs was accompanied by concurrent decreased primary wall CESA and increased secondary wall CESA protein abundance. Our data reveal distinct and dynamic subcellular trafficking patterns that underpin the remodeling of the cellulose biosynthetic machinery, resulting in the removal and degradation of the primary wall CESA complex with concurrent production and recycling of the secondary wall CESAs.

scholarly journals Endosidin20 targets cellulose synthase catalytic domain to inhibit cellulose biosynthesis

2020 ◽  
Author(s):  
Lei Huang ◽  
Xiaohui Li ◽  
Weiwei Zhang ◽  
Nolan Ung ◽  
Nana Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Catalytic Activity ◽  
Catalytic Domain ◽  
Cellulose Synthase ◽  
Catalytic Site ◽  
Cellulose Synthesis ◽  
Spatiotemporal Resolution ◽  
Chemical Genetic ◽  
Biochemical Assays

AbstractCellulose is synthesized by rosette structured cellulose synthase (CESA) complexes (CSCs), each of which is composed of multiple units of CESAs in three different isoforms. CSCs rely on vesicle trafficking for delivery to the plasma membrane where they catalyze cellulose synthesis. Although the rosette structured CSCs were observed decades ago, it remains unclear what amino acids in plant CESA that directly participate in cellulose catalytic synthesis. It is also not clear how the catalytic activity of CSCs influences their efficient transport at the subcellular level. Here we report characterization of the small molecule Endosidin20 (ES20) and present evidence that it represents a new CESA inhibitor. We show data from chemical genetic analyses, biochemical assays, structural modeling, and molecular docking to support our conclusion that ES20 targets the catalytic site of Arabidopsis CESA6. Further, chemical genetic analysis reveals important amino acids that potentially form the catalytic site of plant CESA6. Using high spatiotemporal resolution live-cell imaging, we found that inhibition of CSC catalytic activity by inhibitor treatment, or by creating missense mutation at amino acids in the predicted catalytic site, causes reduced efficiency in CSC transport to the plasma membrane. Our results show that the catalytic activity of plant CSCs is integrated with subcellular trafficking dynamics.One sentence summaryEndosidin20 targets cellulose synthase at the catalytic site to inhibit cellulose synthesis and the inhibition of catalytic activity reduces cellulose synthase complex delivery to the plasma membrane.

scholarly journals A G protein-coupled receptor-like module regulates Cellulose Synthase secretion from the endomembrane system in Arabidopsis

2020 ◽  
Author(s):  
Heather E. McFarlane ◽  
Daniela Mutwil-Anderwald ◽  
Jana Verbančič ◽  
Kelsey L. Picard ◽  
Timothy E. Gookin ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
G Protein ◽  
Protein Complex ◽  
Cellulose Synthase ◽  
Cell Wall Integrity ◽  
Cellulose Synthesis ◽  
Endomembrane System ◽  
G Protein Coupled

AbstractCellulose synthesis is essential for plant morphology, water transport and defense, and provides raw material for biomaterials and fuels. Cellulose is produced at the plasma membrane by Cellulose Synthase (CESA) protein complexes (CSCs). CSCs are assembled in the endomembrane system and then trafficked from the Golgi apparatus and trans-Golgi Network (TGN) to the plasma membrane. Since CESA enzymes are only active in the plasma membrane, control of CSC secretion is a critical step in the regulation of cellulose synthesis. However, the regulatory framework for CSC secretion is not clarified. In this study, we identify members of a family of seven transmembrane domain-containing proteins (7TMs) as important for cellulose production during cell wall integrity stress. 7TM proteins are often associated with guanine nucleotide-binding protein (G) protein signalling and mutants in several of the canonical G protein complex components phenocopied the 7tm mutant plants. Unexpectedly, the 7TM proteins localized to the Golgi apparatus/TGN where they interacted with the G protein complex. Here, the 7TMs and G proteins regulated CESA trafficking, but did not affect general protein secretion. Furthermore, during cell wall stress, 7TMs’ localization was biased towards small CESA-containing vesicles, specifically associated with CSC trafficking. Our results thus outline how a G protein-coupled module regulates CESA trafficking and reveal that defects in this process lead to exacerbated responses upon exposure to cell wall integrity stress.

scholarly journals Gibberellin induced transcription factor bZIP53 regulates CesA1 expression in maize kernels

PLoS ONE ◽  
2021 ◽  
Vol 16 (3) ◽  
pp. e0244591
Author(s):  
Huayang Lv ◽  
Xiao Li ◽  
Hui Li ◽  
Yufeng Hu ◽  
Hanmei Liu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcriptional Activation ◽  
Cellulose Synthase ◽  
Cellulose Synthesis ◽  
Cellulose Content ◽  
Hormone Regulation ◽  
Grain Development ◽  
Cellulose Synthase Gene ◽  
Maize Grain ◽  
Maize Kernels

Proper development of the maize kernel is of great significance for high and stable maize yield to ensure national food security. Gibberellin (GA), one of the hormones regulating plant growth, is involved in modulating the development of maize kernels. Cellulose, one of the main components of plant cells, is also regulated by gibberellin. The mechanism of hormone regulation during maize grain development is highly complicated, and reports on GA-mediated modulation of cellulose synthesis during maize grain development are rare. Our study revealed that during grain growth and development, the grain length and bulk density of GA-treated corn kernels improved significantly, and the cellulose content of grains increased, while seed coat thickness decreased. The transcription factor basic region/leucine zipper motif 53 (bZIP53), which is strongly correlated with cellulose synthase gene 1 (CesA1) expression, was screened by transcriptome sequencing and the expression of the cellulose synthase gene in maize grain development after GA treatment was determined. It was found that bZIP53 expression significantly promoted the expression of CesA1. Further, analysis of the transcription factor bZIP53 determined that the gene-encoded protein was localized in the cell and nuclear membranes, but the transcription factor bZIP53 itself showed no transcriptional activation. Further studies are required to explore the interaction of bZIP53 with CesA1.

scholarly journals Cellulose synthase-like D (CSLD) proteins move in the plasma membrane and their targeting to cell tips, but not cell plates, depends on the actin cytoskeleton

2021 ◽  
Author(s):  
Shu-Zon Wu ◽  
Arielle M. Chaves ◽  
Rongrong Li ◽  
Magdalena Bezanilla ◽  
Alison W. Roberts
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Tip Growth ◽  
Cellulose Synthase ◽  
Live Cell ◽  
Cellulose Microfibrils ◽  
Apical Plasma Membrane ◽  
Cellulose Synthesis

Cellulose Synthase-Like D (CSLD) proteins are implicated in cell wall remodeling during tip growth and cell division in plants, and are known to generate β-1,4-glucan. It is unknown whether they form complexes and move in the plasma membrane like members of the Cellulose Synthase (CESA) family. We used the genetically tractable moss Physcomitrium patens, which has a filamentous protonemal stage that undergoes both tip growth and cell division and is amenable to high resolution live cell imaging, to investigate CSLD function and intracellular trafficking. CSLD2 and CSLD6 are highly expressed in gametophores and are redundantly required for gametophore cellular patterning. Live cell imaging revealed that CSLD6 is also expressed in protonemata where it moves in the plasma membrane and localizes to cell plates and cell tips. Notably, delivery to the apical plasma membrane, but not the cell plate, depends on actin. By comparing the behavior of endogenously tagged CSLD6 and CESA10, we discovered that CSLD6 movements in the plasma membrane were significantly faster, shorter in duration and less linear than CESA10 movements and were insensitive to the cellulose synthesis inhibitor isoxaben. These data suggest that CSLD6 and CESA10 function within different structures and may thus produce structurally distinct cellulose microfibrils.

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