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.
Highlights
V-set and transmembrane domain-containing protein 5 (Vstm5) is a small putative cell-adhesion molecule belonging to the immunoglobulin superfamily abundantly expressed in mouse brain
To determine the glycan maturation of Vstm5 in COS-7 cells at steady state, cell lysates expressing Vstm5::1D4 or Vstm5::green fluorescent protein (GFP) were digested with endoglycosidase H (endo H) or PNGase F to remove the entire glycan chain (Fig 1C and 1D)
We showed that Vstm5, a newly characterized membrane protein, undergoes Nlinked glycosylation at multiple sites
Summary
V-set and transmembrane domain-containing protein 5 (Vstm5) is a small putative cell-adhesion molecule belonging to the immunoglobulin superfamily abundantly expressed in mouse brain. Vstm is highly expressed at postnatal day 1 in mouse brain, when synaptogenesis actively occurs [1]. This temporal expression pattern suggests that Vstm modulates neuronal connectivity and plasticity. Vstm regulates neuronal morphology by redistributing Factin and promotes synapse formation [2]. Vstm promotes neurite formation in the leading processes of migrating neurons to facilitate dendrite formation and integration of neurons into the appropriate laminae of the developing mouse cortex [2].
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