Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/144039
Title: Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking
Authors: Sun, Xiuping
Tie, Hieng Chiong
Chen, Bing
Lu, Lei
Keywords: Science::Biological sciences
Issue Date: 2020
Source: Sun, X., Tie, H. C., Chen, B. & Lu, L. (2020). Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking. Journal of Biological Chemistry. https://dx.doi.org/10.1074/jbc.RA120.014476
Project: MOE AcRF Tier1 RG35/17
Tier2 MOE2015-T2-2-073
Tier2 MOE2018-T2-2- 026
Journal: Journal of Biological Chemistry
Abstract: Most proteins in the secretory pathway are glycosylated. However, the role of glycans in membrane trafficking is still unclear. Here, we discovered that transmembrane secretory cargos, such as interleukin 2 receptor α subunit or Tac, transferrin receptor and cluster of differentiation 8a, unexpectedly displayed substantial Golgi localization when their O-glycosylation was compromised. By quantitatively measuring their Golgi residence times, we found that the observed Golgi localization of O-glycan deficient cargos is due to their slow Golgi export. Using a super-resolution microscopy method that we previously developed, we revealed that O-glycan deficient Tac chimeras localize at the interior of the trans-Golgi cisternae. O-glycans were observed to be both necessary and sufficient for the efficient Golgi export of Tac chimeras. By sequentially introducing O-glycosylation sites to ST6GAL1, we demonstrated that O-glycan’s effect on Golgi export is probably additive. Finally, the finding that N-glycosylated GFP substantially reduces the Golgi residence time of a Tac chimera suggests that N-glycans might have a similar effect. Therefore, both O- and N-glycans might function as a generic Golgi export signal at the trans-Golgi to promote the constitutive exocytic trafficking.
URI: https://hdl.handle.net/10356/144039
ISSN: 0021-9258
DOI: 10.1074/jbc.RA120.014476
Rights: © 2020 American Society for Biochemistry and Molecular Biology. All rights reserved. This paper was published in Journal of Biological Chemistry and is made available with permission of American Society for Biochemistry and Molecular Biology.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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