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Title: A quantitative study of the Golgi retention of glycosyltransferases
Authors: Sun, Xiuping
Mahajan, Divyanshu
Chen, Bing
Song, Zhiwei
Lu, Lei
Keywords: Science::Biological sciences
Issue Date: 2021
Source: Sun, X., Mahajan, D., Chen, B., Song, Z. & Lu, L. (2021). A quantitative study of the Golgi retention of glycosyltransferases. Journal of Cell Science, 134(20), jcs258564-.
Project: MOE AcRF Tier1 RG35/17
MOE2018-T2-2- 026 to L.L
Journal: Journal of Cell Science
Abstract: How Golgi glycosyltransferases and glycosidases (hereafter glycosyltransferases) localize to the Golgi is still unclear. Here, we first investigated the post-Golgi trafficking of glycosyltransferases. We found that glycosyltransferases can escape the Golgi to the plasma membrane, where they are subsequently endocytosed to the endolysosome. Post-Golgi glycosyltransferases are probably degraded by ectodomain shedding. We discovered that most glycosyltransferases are not retrieved from post-Golgi sites, indicating that retention rather than retrieval is the primary mechanism for their Golgi localization. We therefore used the Golgi residence time to study Golgi retention of glycosyltransferases quantitatively and systematically. Quantitative analysis of chimeras of ST6GAL1 and either transferrin receptor or tumor necrosis factor α revealed the contributions of three regions of ST6GAL1, namely the N-terminal cytosolic tail, the transmembrane domain and the ectodomain, to Golgi retention. We found that each of the three regions is sufficient for Golgi retention in an additive manner. N-terminal cytosolic tail length negatively affects the Golgi retention of ST6GAL1, similar to effects observed for the transmembrane domain. Therefore, the long N-terminal cytosolic tail and transmembrane domain could act as Golgi export signals for transmembrane secretory cargos. This article has an associated First Person interview with the first author of the paper.
ISSN: 0021-9533
DOI: 10.1242/jcs.258564
Rights: © 2021 The Author(s). All rights reserved. This paper was published by The Company of Biologists Ltd. in Journal of Cell Science and is made available with permission of The Author(s).
Fulltext Permission: embargo_20221028
Fulltext Availability: With Fulltext
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