ArticleCommunications biology2022
An embeddable molecular code for Lewis X modification through interaction with fucosyltransferase 9.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 7 citations in OpenAlex.
- The protein sequence modulates terminal GalNAc incorporation during N-glycan biosynthesis.Glycobiology · 2026Article
- Dynamic inter-glycan interactions regulate site-specific N-glycan maturation in human Fcγ receptor III.Glycobiology · 2026Article
- Regulation of Glycan Modification by Glycosyltransferases in the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Distinct brain alterations and neurodegenerative processes in cognitive impairment associated with post-acute sequelae of COVID-19.Nature communications · 2025Article
- Molecular tag for promotingiScience · 2024Article
- Deciphering the sub-Golgi localization of glycosyltransferases via 3D super-resolution imaging.Cell structure and function · 2024Article
- The impact of glycosylation on the structure, function, and interactions of CD14.Glycobiology · 2024Article
- Impact of N-Linked Glycosylation on Therapeutic Proteins.Molecules (Basel, Switzerland) · 2022Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-glycans are diversified by a panel of glycosyltransferases in the Golgi, which are supposed to modify various glycoproteins in promiscuous manners, resulting in unpredictable glycosylation profiles in general. In contrast, our previous study showed that fucosyltransferase 9 (FUT9) generates Lewis X glycotopes primarily on lysosome-associated membrane protein 1 (LAMP-1) in neural stem cells. Here, we demonstrate that a contiguous 29-amino acid sequence in the N-terminal domain of LAMP-1 is responsible for promotion of the FUT9-catalyzed Lewis X modification. Interestingly, Lewis X modification was induced on erythropoietin as a model glycoprotein both in vitro and in cells, just by attaching this sequence to its C-terminus. Based on these results, we conclude that the amino acid sequence from LAMP-1 functions as a "Lewis X code", which is deciphered by FUT9, and can be embedded into other glycoproteins to evoke a Lewis X modification, opening up new possibilities for protein engineering and cell engineering.
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