Structural basis of nucleotide sugar transport across the Golgi membrane
Glycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum1. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for th...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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Springer Nature
2017
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| _version_ | 1797068710631964672 |
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| author | Parker, J Newstead, S |
| author_facet | Parker, J Newstead, S |
| author_sort | Parker, J |
| collection | OXFORD |
| description | Glycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum1. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for the glycosyltransferases2,3. NSTs are linked to several developmental and immune disorders in humans, and in pathogenic microbes they have an important role in virulence4,5,6,7,8. How NSTs recognize and transport activated monosaccharides, however, is currently unclear. Here we present the crystal structure of an NST, the GDP–mannose transporter Vrg4, in both the substrate-free and the bound states. A hitherto unobserved requirement of short-chain lipids in activating the transporter supports a model for regulation within the highly dynamic membranes of the Golgi apparatus. Our results provide a structural basis for understanding nucleotide sugar recognition, and provide insights into the transport and regulatory mechanism of this family of intracellular transporters. |
| first_indexed | 2024-03-06T22:14:06Z |
| format | Journal article |
| id | oxford-uuid:52d171bc-7ef6-498d-ad29-16fed05f0871 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:14:06Z |
| publishDate | 2017 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:52d171bc-7ef6-498d-ad29-16fed05f08712022-03-26T16:27:40ZStructural basis of nucleotide sugar transport across the Golgi membraneJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:52d171bc-7ef6-498d-ad29-16fed05f0871EnglishSymplectic Elements at OxfordSpringer Nature2017Parker, JNewstead, SGlycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum1. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for the glycosyltransferases2,3. NSTs are linked to several developmental and immune disorders in humans, and in pathogenic microbes they have an important role in virulence4,5,6,7,8. How NSTs recognize and transport activated monosaccharides, however, is currently unclear. Here we present the crystal structure of an NST, the GDP–mannose transporter Vrg4, in both the substrate-free and the bound states. A hitherto unobserved requirement of short-chain lipids in activating the transporter supports a model for regulation within the highly dynamic membranes of the Golgi apparatus. Our results provide a structural basis for understanding nucleotide sugar recognition, and provide insights into the transport and regulatory mechanism of this family of intracellular transporters. |
| spellingShingle | Parker, J Newstead, S Structural basis of nucleotide sugar transport across the Golgi membrane |
| title | Structural basis of nucleotide sugar transport across the Golgi membrane |
| title_full | Structural basis of nucleotide sugar transport across the Golgi membrane |
| title_fullStr | Structural basis of nucleotide sugar transport across the Golgi membrane |
| title_full_unstemmed | Structural basis of nucleotide sugar transport across the Golgi membrane |
| title_short | Structural basis of nucleotide sugar transport across the Golgi membrane |
| title_sort | structural basis of nucleotide sugar transport across the golgi membrane |
| work_keys_str_mv | AT parkerj structuralbasisofnucleotidesugartransportacrossthegolgimembrane AT newsteads structuralbasisofnucleotidesugartransportacrossthegolgimembrane |