ArticlePloS one2017
Differential effects of N-linked glycosylation of Vstm5 at multiple sites on surface expression and filopodia formation.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Detection and Visualization of Heterozygosity-Rich Regions and Runs of Homozygosity in Worldwide Sheep Populations.Animals : an open access journal from MDPI · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
V-set and transmembrane domain-containing protein 5 (Vstm5), a newly characterized small membrane glycoprotein, can induce membrane protrusions in various cells. Vstm5 can modulate both the position and complexity of central neurons by altering their membrane morphology and dynamics. In this study, we investigated the significance of glycosylation in the expression and function of Vstm5. Four N-linked glycosylation sites (Asn43, Asn87, Asn101, and Asn108) are predicted to be located in the extracellular N-terminus of mouse Vstm5. Although all four sites were glycosylated, their functional roles may not be identical. N-glycosylation at multiple sites affects differentially the function of Vstm5. Glycosylation at individual sites not only played essential roles in surface expression of Vstm5 but also in the formation of neuronal dendritic filopodia. These results indicate that N-linked glycosylation at multiple sites plays important roles by differentially influencing the expression, targeting, and biological activity of Vstm5.
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Registered trials
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