Abstract

Glycosyl Modification Facilitates Homo- and Hetero-oligomerization of the Serotonin Transporter: A SPECIFIC ROLE FOR SIALIC ACID RESIDUESJournal of Biological ChemistryVol. 278Issue 45PreviewThe serotonin transporter (SERT) is an oligomeric glycoprotein with two sialic acid residues on each of two complex oligosaccharide molecules. In this study, we investigated the contribution of N-glycosyl modification to the structure and function of SERT in two model systems: wild-type SERT expressed in sialic acid-defective Lec Chinese hamster ovary (CHO) cells and a mutant form (after site-directed mutagenesis of Asn-208 and Asn-217 to Gln) of SERT, QQ, expressed in parental CHO cells. In both systems, SERT monomers required modification with both complex oligosaccharide residues to associate with each other and to function in homo-oligomeric forms. Full-Text PDF Open Access VOLUME 278 (2003) PAGES 43991–44000 The publisher of the Journal of Biological Chemistry is issuing an Expression of Concern to inform readers that credible concerns have been raised regarding some of the data and conclusions in the article listed above. The Journal of Biological Chemistry will provide additional information as it becomes available.

Highlights

  • The publisher of the Journal of Biological Chemistry is issuing an Expression of Concern to inform readers that credible concerns have been raised regarding some of the data and conclusions in the article listed above

  • The Journal of Biological Chemistry will provide additional information as it becomes available

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