title: The elaborate route for UDP-arabinose delivery into the Golgi of plants.
abstract: In plants, L-arabinose (Ara) is a key component of cell wall polymers, glycoproteins, as well as flavonoids, and signaling peptides. Whereas the majority of Ara found in plant glycans occurs as a furanose ring (Araf), the activated precursor has a pyranose ring configuration (UDP-Arap). The biosynthesis of UDP-Arapmainly occurs via the epimerization of UDP-xylose (UDP-Xyl) in the Golgi lumen. Given that the predominant Ara form found in plants is Araf, UDP-Arapmust exit the Golgi to be interconverted into UDP-Arafby UDP-Ara mutases that are located outside on the cytosolic surface of the Golgi. Subsequently, UDP-Arafmust be transported back into the lumen. This step is vital because glycosyltransferases, the enzymes mediating the glycosylation reactions, are located within the Golgi lumen, and UDP-Arap, synthesized within the Golgi, is not their preferred substrate. Thus, the transport of UDP-Arafinto the Golgi is a prerequisite. Although this step is critical for cell wall biosynthesis and the glycosylation of proteins and signaling peptides, the identification of these transporters has remained elusive. In this study, we present data demonstrating the identification and characterization of a family of Golgi-localized UDP-Araftransporters inArabidopsisThe application of a proteoliposome-based transport assay revealed that four members of the nucleotide sugar transporter (NST) family can efficiently transport UDP-Arafin vitro. Subsequent analysis of mutant lines affected in the function of these NSTs confirmed their role as UDP-Araftransporters in vivo.
authors.affiliation: School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia.|Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702.
authors.forename: Carsten
authors.initials: C
authors.lastname: Rautengarten
authors.affiliation: Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702.
authors.forename: Devon
authors.initials: D
authors.lastname: Birdseye
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
authors.forename: Sivakumar
authors.initials: S
authors.lastname: Pattathil
authors.affiliation: School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia.
authors.forename: Heather E
authors.initials: HE
authors.lastname: McFarlane
authors.affiliation: Centro de Biotecnología Vegetal, Fondo de Areas Prioritarias Center for Genome Regulation, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago RM 8370146, Chile.
authors.forename: Susana
authors.initials: S
authors.lastname: Saez-Aguayo
authors.affiliation: Centro de Biotecnología Vegetal, Fondo de Areas Prioritarias Center for Genome Regulation, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Santiago RM 8370146, Chile.
authors.forename: Ariel
authors.initials: A
authors.lastname: Orellana
authors.affiliation: School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia.
authors.forename: Staffan
authors.initials: S
authors.lastname: Persson
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
authors.forename: Michael G
authors.identifier: 0000-0003-2136-5191
authors.initials: MG
authors.lastname: Hahn
authors.affiliation: Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702.|Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720.
authors.forename: Henrik V
authors.initials: HV
authors.lastname: Scheller
authors.affiliation: School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia.|Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702.
authors.forename: Joshua L
authors.identifier: 0000-0002-2080-3826
authors.initials: JL
authors.lastname: Heazlewood
authors.affiliation: School of BioSciences, The University of Melbourne, Melbourne, VIC 3010, Australia; berit.ebert@unimelb.edu.au.|Joint BioEnergy Institute, Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94702.
authors.forename: Berit
authors.initials: B
authors.lastname: Ebert
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D002473:Cell Wall / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D006056:Golgi Apparatus / Q000378:metabolism*; D014539:Uridine Diphosphate Sugars / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; D014539:Uridine Diphosphate Sugars; C040817:uridine diphosphate arabinose
keywords: Golgi apparatus; arabinose; membrane transport; nucleotide sugars