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Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking
- Source :
- The Journal of Biological Chemistry
- Publication Year :
- 2020
- Publisher :
- Elsevier BV, 2020.
-
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. Ministry of Education (MOE) This work was supported by the following grants to L.L.: MOE AcRF Tier1 RG35/17, Tier2 MOE2015-T2-2-073 and Tier2 MOE2018-T2-2- 026.
- Subjects :
- 0301 basic medicine
Glycan
Glycosylation
intracellular trafficking
CD8 Antigens
Golgi export
Golgi Apparatus
Transferrin receptor
N-glycosylation
Biochemistry
Exocytosis
Green fluorescent protein
03 medical and health sciences
symbols.namesake
chemistry.chemical_compound
N-linked glycosylation
Polysaccharides
constitutive exocytosis
Receptors, Transferrin
Golgi
Humans
membrane protein
Receptor
Golgi localization
Molecular Biology
Secretory pathway
O-glycosylation
biology
030102 biochemistry & molecular biology
membrane trafficking
Interleukin-2 Receptor alpha Subunit
Biological sciences [Science]
imaging
Cell Biology
Golgi apparatus
protein trafficking (Golgi)
Transmembrane protein
secretory pathway
Cell biology
carbohydrates (lipids)
Protein Transport
030104 developmental biology
chemistry
biology.protein
symbols
HeLa Cells
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 295
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....211dc7368a1d7504459f3226828ee19c