Cellulose synthase interactive protein 1 (CSI1) links microtubules and cellulose synthase complexes.
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ABSTRACT:
SUBMITTER: Li S
PROVIDER: S-EPMC3252916 | biostudies-literature |
REPOSITORIES: biostudies-literature
Similar Datasets
Project description:We compared the transcriptome of homozygous mutants for AtCesA4 and AtCesA6 (cellulose synthase genes) to their heterozygous counterparts that have a wild type phenotype. All plants were 4-weeks-old and grown under short day conditions.
2010-04-19 | GSE20221 | GEO
Project description:We compared the transcriptome of homozygous mutants for AtCesA4 and AtCesA6 (cellulose synthase genes) to their heterozygous counterparts that have a wild type phenotype. All plants were 4-weeks-old and grown under short day conditions. 10 samples were used in this experiment: 3 each homozygous and heterozygous AtCesA4 plants, and 2 each homozygous and heterozygous AtCesA6 plants.
2010-04-28 | E-GEOD-20221 | biostudies-arrayexpress
Project description: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.
| S-EPMC6142216 | biostudies-literature
Project description:Cellulose synthase-interactive protein 1 (CSI1) was identified in a two-hybrid screen for proteins that interact with cellulose synthase (CESA) isoforms involved in primary plant cell wall synthesis. CSI1 encodes a 2,150-amino acid protein that contains 10 predicted Armadillo repeats and a C2 domain. Mutations in CSI1 cause defective cell elongation in hypocotyls and roots and reduce cellulose content. CSI1 is associated with CESA complexes, and csi1 mutants affect the distribution and movement of CESA complexes in the plasma membrane.
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Project description:Helical growth is an economical way for plant to obtain resources. The classic microtubule-microfibril alignment model of Arabidopsis helical growth involves restriction of the appropriate orientation of cellulose microfibrils appropriately in the cell walls. However, the molecular mechanism underlying tomato helical growth remains unknown. Here, we identified a spontaneous tomato helical (hel) mutant with right-handed helical cotyledons and petals but left-handed helical stems and true leaves. Genetic analysis revealed that the hel phenotype was controlled by a single recessive gene. Using map-based cloning, we cloned the HEL gene, which encodes a cellulose interacting protein homologous to CSI1 of Arabidopsis. We identified a 27 bp fragment replacement that generated a premature stop codon. Transgenic experiments showed that the helical growth phenotype could be restored by the allele of this gene from wild-type Pyriforme. In contrast, the knockout mutation of HEL in Pyriforme via CRISPR/Cas9 resulted in helical growth. These findings shed light on the molecular control of the helical growth of tomato.
| S-EPMC7603515 | biostudies-literature
Project description:In all land plants, cellulose is synthesized from hexameric plasma membrane complexes. Indirect evidence suggests that in vascular plants the complexes involved in primary wall synthesis contain three distinct cellulose synthase catalytic subunits (CESAs). In this study, we show that CESA3 and CESA6 fused to GFP are expressed in the same cells and at the same time in the hypocotyl of etiolated seedlings and migrate with comparable velocities along linear trajectories at the cell surface. We also show that CESA3 and CESA6 can be coimmunoprecipitated from detergent-solubilized extracts, their protein levels decrease in mutants for either CESA3, CESA6, or CESA1 and CESA3, CESA6 and also CESA1 can physically interact in vivo as shown by bimolecular fluorescence complementation. We also demonstrate that CESA6-related CESA5 and CESA2 are partially, but not completely, redundant with CESA6 and most likely compete with CESA6 for the same position in the cellulose synthesis complex. Using promoter-beta-glucuronidase fusions we show that CESA5, CESA6, and CESA2 have distinct overlapping expression patterns in hypocotyl and root corresponding to different stages of cellular development. Together, these data provide evidence for the existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position. Participation of the latter three isoforms might fine-tune the CESA complexes for the deposition of microfibrils at distinct cellular growth stages.
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Project description:Cellulose, the most abundant biopolymer on the planet, is synthesized at the plasma membrane of plant cells by the cellulose synthase complex (CSC). Cellulose is the primary load-bearing polysaccharide of plant cell walls and enables cell walls to maintain cellular shape and rigidity. The CSC is comprised of functionally distinct cellulose synthase A (CESA) proteins, which are responsible for synthesizing cellulose, and additional accessory proteins. Moreover, CESA-like (CSL) proteins are proposed to synthesize other essential non-cellulosic polysaccharides that comprise plant cell walls. The deposition of cell-wall polysaccharides is dynamically regulated in response to a variety of developmental and environmental stimuli, and post-translational phosphorylation has been proposed as one mechanism to mediate this dynamic regulation. In this review, we discuss CSC composition, the dynamics of CSCs in vivo, critical studies that highlight the post-translational control of CESAs and CSLs, and the receptor kinases implicated in plant cell-wall biosynthesis. Furthermore, we highlight the emerging importance of post-translational phosphorylation-based regulation of CSCs on the basis of current knowledge in the field.
| S-EPMC6161211 | biostudies-literature
Project description:As the most abundant biopolymer on Earth, cellulose is a key structural component of the plant cell wall. Cellulose is produced at the plasma membrane by cellulose synthase (CesA) complexes (CSCs), which are assembled in the endomembrane system and trafficked to the plasma membrane. While several proteins that affect CesA activity have been identified, components that regulate CSC assembly and trafficking remain unknown. Here we show that STELLO1 and 2 are Golgi-localized proteins that can interact with CesAs and control cellulose quantity. In the absence of STELLO function, the spatial distribution within the Golgi, secretion and activity of the CSCs are impaired indicating a central role of the STELLO proteins in CSC assembly. Point mutations in the predicted catalytic domains of the STELLO proteins indicate that they are glycosyltransferases facing the Golgi lumen. Hence, we have uncovered proteins that regulate CSC assembly in the plant Golgi apparatus.
| S-EPMC4906169 | biostudies-literature
Project description:In higher plants, cellulose is synthesized at the plasma membrane by the cellulose synthase (CESA) complex. The catalytic core of the complex is believed to be composed of three types of CESA subunits. Indirect evidence suggests that the complex associated with primary wall cellulose deposition consists of CESA1, -3, and -6 in Arabidopsis thaliana. However, phenotypes associated with mutations in two of these genes, CESA1 and -6, suggest unequal contribution by the different CESAs to overall enzymatic activity of the complex. We present evidence that the primary complex requires three unique types of components, CESA1-, CESA3-, and CESA6-related, for activity. Removal of any of these components results in gametophytic lethality due to pollen defects, demonstrating that primary-wall cellulose synthesis is necessary for pollen development. We also show that the CESA6-related CESAs are partially functionally redundant.
| S-EPMC2000526 | biostudies-literature
Project description:Cellulose is a cell wall constituent that is essential for plant growth and development, and an important raw material for a range of industrial applications. Cellulose is synthesized at the plasma membrane by massive cellulose synthase (CesA) complexes that track along cortical microtubules in elongating cells of Arabidopsis through the activity of the protein CELLULOSE SYNTHASE INTERACTING1 (CSI1). In a recent study we identified another family of proteins that also are associated with the CesA complex and microtubules, and that we named COMPANIONS OF CELLULOSE SYNTHASE (CC). The CC proteins protect the cellulose synthesising capacity of Arabidopsis seedlings during exposure to adverse environmental conditions by enhancing microtubule dynamics. In this paper we provide cell biology and genetic evidence that the CSI1 and the CC proteins fulfil distinct functions during cellulose synthesis. We also show that the CC proteins are necessary to aid cellulose synthesis when components of the CesA complex are impaired. These data indicate that the CC proteins have a broad role in aiding cellulose synthesis during environmental changes and when core complex components are non-functional.
| S-EPMC4883956 | biostudies-other