SuSy <i>ergo</i> GluSy: New Developments in the Field of Cellulose Biosynthesis

Robinson, David G.

doi:10.1111/j.1438-8677.1996.tb00571.x

Cited by 11 publications

(5 citation statements)

References 21 publications

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“…The increased membrane association may be necessary to support the increased cell wall deposition required for rapid cell elongation in the pulvinus (especially the lower surface). This would be entirely consistent with the notion that membrane-bound SuSy channels UDP-glucose formed during Suc cleavage to cellulose synthase [6,8]. The second major conclusion is that phosphorylation of SuSy may be at least part of the mechanism controlling SuSy localization, and is supported by three lines of evidence: (i) dephosphorylation of SuSy causes increased association with the membrane fraction; (ii) phosphorylation of membrane proteins caused the release of SuSy from the membrane; and (iii) in vivo phosphorylation studies indicate that the membrane-associated enzyme contains less QP P than the soluble enzyme (SuSy protein basis).…”

Section: Resultssupporting

confidence: 87%

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Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

1997

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Sucrose synthase (SuSy) plays an important role in sucrose degradation and occurs both as a soluble and as a membrane-associated enzyme in higher plants. We show that membrane association can vary in vivo in response to gravistimulation, apparently involving SuSy dephosphorylation, and is a reversible process in vitro. Phosphorylation of SuSy has little effect on its activity but decreases its surface hydrophobicity as reported with the fluorescent probe bis-ANS. We postulate that phosphorylation of SuSy (and perhaps other membrane proteins) is involved in the release of the membrane-bound enzyme in part as a result of decreased surface hydrophobicity.z 1997 Federation of European Biochemical Societies.

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Section: Resultssupporting

confidence: 87%

“…Recently, it was found that some of the SuSy protein is associated with the plasma membrane and it was postulated that it may exist in a complex with β‐glucan synthases to channel UDP‐glucose into glucan (e.g. cellulose) synthesis [6–8]. SuSy has been shown to be phosphorylated in maize leaves [9]and soybean nodules [10].…”

Section: Introductionmentioning

confidence: 99%

Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

1997

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“…A membrane-associated form of SuSy has recently been identified in a number of plants (4,23,135). We proposed that this form of SuSy might interact with the cellulose synthase to directly channel carbon from sucrose via UDP-glc for the CeSA subunit (4,36,102). However, from our limited studies to date (P Hogan & D Delmer, unpublished data), we have found no evidence for interaction of SuSy with any of the plant-specific domains of CeSA.…”

Section: Interaction Of Cesa Polypeptides With Other Proteinsmentioning

confidence: 62%

CELLULOSE BIOSYNTHESIS: Exciting Times for A Difficult Field of Study

Delmer

1999

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

590

517

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The past few decades have witnessed exciting progress in studies on the biosynthesis of cellulose. In the bacterium Acetobacter xylinum, discovery of the activator of the cellulose synthase, cyclic diguanylic acid, opened the way for obtaining high rates of in vitro synthesis of cellulose. This, in turn, led to purification of the cellulose synthase and for the cloning of genes that encode the catalytic subunit and other proteins that bind the activator and regulate its synthesis and degradation, or that control secretion and crystallization of the microfibrils. In higher plants, a family of genes has been discovered that show interesting similarities and differences from the gene in bacteria that encodes the catalytic subunit of the synthase. Genetic evidence now supports the concept that members of this family encode the catalytic subunit in these organisms, with various members showing tissue-specific expression. Although the cellulose synthase has not yet been purified to homogeneity from plants, recent progress in this area suggests that this will soon be accomplished.

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“…The mechanism of cellulose biosynthesis in higher plants is only poorly understood. It has been proposed that the membrane-bound SS exists in a complex with the b-glucan synthases; this sucrose-cleaving enzyme may provide UDP-glucose as a substrate for cellulose biosynthesis , Robinson 1996. The 'Susy-Glusy-model' of cellulose apposition was originally formulated on the basis of Fig.…”

Section: Discussionmentioning

confidence: 99%

Sucrose metabolism and cellulose biosynthesis in sunflower hypocotyls

Kutschera¹,

Heiderich²

2002

Physiologia Plantarum

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The relationships between cellulose accumulation, changes in specific activities of enzymes of sucrose catabolism, levels of UDP-glucose and rate of dark respiration were investigated in the subapical 1 cm-hypocotyl region of 10- to 14-day-old-sunflower seedlings (Helianthus annuus L). The plants were grown under a light/dark regime in vermiculite that was soaked either with distilled water or half-strength Hoagland nutrient solution. At this stage of seedling development, the hypocotyl had ceased to elongate but increased in width. Stem thickening and the rate of cellulose accumulation were promoted by nutrient solution. The levels of the soluble (vacuolar) and wall-associated acid invertases (EC 3.2.1.26) were not correlated with these processes. However, the activities of the soluble (cytoplasmic) and membrane-bound sucrose synthases (EC 2.4.1.13) were larger in hypocotyls that were grown in the presence of nutrient solution. The concentration of UDP-glucose was reduced, and the rate of dark respiration was enhanced in the hypocotyls that were grown in Hoagland solution. The results support the hypothesis that both forms of the enzyme sucrose synthase play a critical role in cellulose biosynthesis of hypocotyl cells that had ceased to elongate and continue to grow by wall thickening.

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SuSy ergo GluSy: New Developments in the Field of Cellulose Biosynthesis

Cited by 11 publications

References 21 publications

Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

Membrane association of sucrose synthase: changes during the graviresponse and possible control by protein phosphorylation

CELLULOSE BIOSYNTHESIS: Exciting Times for A Difficult Field of Study

Sucrose metabolism and cellulose biosynthesis in sunflower hypocotyls

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