ArticlePlant physiology2000
GDP-fucose uptake into the Golgi apparatus during xyloglucan biosynthesis requires the activity of a transporter-like protein other than the UDP-glucose transporter.
Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- New steps in mucilage biosynthesis revealed by analysis of the transcriptome of the UDP-rhamnose/UDP-galactose transporter 2 mutant.Journal of experimental botany · 2019Article
- UUAT1 Is a Golgi-Localized UDP-Uronic Acid Transporter That Modulates the Polysaccharide Composition of Arabidopsis Seed Mucilage.The Plant cell · 2017Article
- The Arabidopsis Golgi-localized GDP-L-fucose transporter is required for plant development.Nature communications · 2016Article
- Abnormal glycosphingolipid mannosylation triggers salicylic acid-mediated responses in Arabidopsis.The Plant cell · 2013Article
- GO-PROMTO illuminates protein membrane topologies of glycan biosynthetic enzymes in the Golgi apparatus of living tissues.PloS one · 2012Article
- Golgi nucleotide sugar transporter modulates cell wall biosynthesis and plant growth in rice.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- The import of S-adenosylmethionine into the Golgi apparatus is required for the methylation of homogalacturonan.Plant physiology · 2007Article
- Article
- Arabidopsis thaliana expresses multiple Golgi-localised nucleotide-sugar transporters related to GONST1.Molecular genetics and genomics : MGG · 2004Article
- Article
- Localisation and characterisation of cell wall mannan polysaccharides in Arabidopsis thaliana.Planta · 2003Article
- Analysis of xyloglucan fucosylation in Arabidopsis.Plant physiology · 2003Article
- Analysis of the plastidic phosphate translocator gene family in Arabidopsis and identification of new phosphate translocator-homologous transporters, classified by their putative substrate-binding site.Plant physiology · 2003Article
- A thapsigargin-sensitive Ca(2+) pump is present in the pea Golgi apparatus membrane.Plant physiology · 2002Article
- Identification and characterization of GONST1, a golgi-localized GDP-mannose transporter in Arabidopsis.The Plant cell · 2001Article
- Unravelling cell wall formation in the woody dicot stem.Plant molecular biology · 2001Review
- The catalytic site of the pectin biosynthetic enzyme alpha-1,4-galacturonosyltransferase is located in the lumen of the Golgi.Plant physiology · 2001Article
- Golgi enzymes that synthesize plant cell wall polysaccharides: finding and evaluating candidates in the genomic era.Plant molecular biology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular mechanisms regulating hemicelluloses and pectin biosynthesis are poorly understood. An important question in this regard is how glycosyltransferases are oriented in the Golgi cisternae, and how nucleotide sugars are made available for the synthesis of the polymers. Here we show that the branching enzyme xyloglucan alpha,1-2 fucosyltransferase (XG-FucTase) from growing pea (Pisum sativum) epicotyls was latent and protected against proteolytic inactivation on intact, right-side-in pea stem Golgi vesicles. Moreover, much of the XG-FucTase activity was membrane associated. These data indicate that XG-FucTase is a membrane-bound luminal enzyme. GDP-Fuc uptake studies demonstrated that GDP-Fuc was taken up into Golgi vesicles in a protein-mediated process, and that this uptake was not competed by UDP-Glc, suggesting that a specific GDP-Fuc transporter is involved in xyloglucan biosynthesis. Once in the lumen, Fuc was transferred onto endogenous acceptors, including xyloglucan. GDPase activity was detected in the lumen of the vesicles, suggesting than the GDP produced upon transfer of Fuc was hydrolyzed to GMP and inorganic phosphate. We suggest than the GDP-Fuc transporter and GDPase may be regulators of xyloglucan fucosylation in the Golgi apparatus from pea epicotyls.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.