Advertisement

Nucleotide Sugar Transporter Genes and Their Functional Analysis

  • Shoko Nishihara

Abstract

Carbohydrate structures on glycoproteins and glycolipids play important roles in various biological processes, such as morphogenesis/organ development, viral and bacterial infections/immune response, and cancer invasion. Nucleotide sugar transporters (NSTs) are crucial components in the synthesis of glycoconjugates (Fig. 1) (Caffaro and Hirschberg 2006). Glycosylation can be performed by various types of glycosyltransferase in the lumens of the endoplasmic reticulum and the Golgi apparatus. All glycosyltransferases require donor sugars activated by the addition of a nucleoside mono- or diphosphate (UDP, GDP, or CMP), that is, nucleotide sugars. Nucleotide sugars are synthesized in the cytosol (or in the nucleus in the case of CMP-sialic acid). The translocation of nucleotide sugars from the cytosol into the lumen compartment is mediated by specific NSTs. NSTs are multiple-membrane-spanning proteins that transport nucleotide sugars in coupling with the antiport of nucleoside monophosphate (NMP), which is produced as the result of a glycosyltransferase reaction and a subsequent luminal nucleoside diphosphatase (NDPase) reaction. Recently, NSTs have been suggested to be possible crucial players in the synthesis of glycoconjugates (Suda et al. 2004; Caffaro and Hirschberg 2006).

Keywords

Nucleotide Sugar shRNA Expression Vector Nucleotide Sugar Transporter Golgi Lumen Donor Nucleotide Sugar 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Caffaro CE, Hirschberg CB (2006) Nucleotide sugar transporters of the Golgi apparatus: from basic science to diseases. Acc Chem Res 39:805–812PubMedCrossRefGoogle Scholar
  2. Goda E, Kamiyama S, Uno T, Yoshida H, Ueyama M, Kinoshita-Toyoda A, Toyoda H, Ueda R, Nishihara S (2006) Identification and characterization of a novel Drosophila 3′-phosphoadenosine 5′-phosphosulfate transporter. J Biol Chem 281:28508–28517PubMedCrossRefGoogle Scholar
  3. Kamiyama S, Suda T, Ueda R, Suzuki M, Okubo R, Kikuchi N, Chiba Y, Goto S, Toyoda H, Saigo K, Watanabe M, Narimatsu H, Jigami Y, Nishihara S (2003) Molecular cloning and identification of 3′-phosphoadenosine 5′-phosphosulfate transporter. J Biol Chem 278:25958–25963PubMedCrossRefGoogle Scholar
  4. Kamiyama S, Sasaki N, Goda E, Ui-Tei K, Saigo K, Narimatsu H, Jigami Y, Kannagi R, Irimura T, Nishihara S (2006) Molecular cloning and characterization of a novel 3′-phosphoadenosine 5′-phosphosulfate transporter, PAPST2. J Biol Chem 281:10945–10953PubMedCrossRefGoogle Scholar
  5. Suda T, Kamiyama S, Suzuki M, Kikuchi N, Nakayama K, Narimatsu H, Jigami Y, Aoki T, Nishihara S (2004) Molecular cloning and characterization of a human multisubstrate specific nucleotide-sugar transporter homologous to Drosophila fringe connection. J Biol Chem 279:26469–26474PubMedCrossRefGoogle Scholar

Copyright information

© Springer 2008

Authors and Affiliations

  • Shoko Nishihara
    • 1
  1. 1.Laboratory of Cell Biology, Department of Bioinformatics, Faculty of EngineeringSoka UniversityHachioji, TokyoJapan

Personalised recommendations