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Structural basis for the delivery of activated sialic acid into Golgi for sialyation
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0001-6991-1046
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0960-994X
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 52019 (English)In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 26, no 6, p. 415-423Article in journal (Refereed) Published
Abstract [en]

The decoration of secretory glycoproteins and glycolipids with sialic acid is critical to many physiological and pathological processes. Sialyation is dependent on a continuous supply of sialic acid into Golgi organelles in the form of CMP-sialic acid. Translocation of CMP-sialic acid into Golgi is carried out by the CMP-sialic acid transporter (CST). Mutations in human CST are linked to glycosylation disorders, and CST is important for glycopathway engineering, as it is critical for sialyation efficiency of therapeutic glycoproteins. The mechanism of how CMP-sialic acid is recognized and translocated across Golgi membranes in exchange for CMP is poorly understood. Here we have determined the crystal structure of a Zea mays CST in complex with CMP. We conclude that the specificity of CST for CMP-sialic acid is established by the recognition of the nucleotide CMP to such an extent that they are mechanistically capable of both passive and coupled antiporter activity.

Place, publisher, year, edition, pages
2019. Vol. 26, no 6, p. 415-423
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Biological Sciences
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URN: urn:nbn:se:su:diva-170105DOI: 10.1038/s41594-019-0225-yISI: 000470110200006PubMedID: 31133698OAI: oai:DiVA.org:su-170105DiVA, id: diva2:1334420
Available from: 2019-07-02 Created: 2019-07-02 Last updated: 2019-07-02Bibliographically approved

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Nji, EmmanuelGulati, AshutoshQureshi, Abdul AzizCoincon, MathieuDrew, David
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