{Reference Type}: Journal Article
{Title}: Pre-B cell receptor acts as a selectivity switch for galectin-1 at the pre-B cell surface.
{Author}: Touarin P;Serrano B;Courbois A;Bornet O;Chen Q;Scott LG;Williamson JR;Sebban-Kreuzer C;Mancini SJC;Elantak L;
{Journal}: Cell Rep
{Volume}: 43
{Issue}: 8
{Year}: 2024 Aug 27
暂无{DOI}: 10.1016/j.celrep.2024.114541
{Abstract}: Galectins are glycan-binding proteins translating the sugar-encoded information of cellular glycoconjugates into physiological activities, including immunity, cell migration, and signaling. Galectins also interact with non-glycosylated partners in the extracellular milieu, among which the pre-B cell receptor (pre-BCR) during B cell development. How these interactions might interplay with the glycan-decoding function of galectins is unknown. Here, we perform NMR experiments on native membranes to monitor Gal-1 binding to physiological cell surface ligands. We show that pre-BCR interaction changes Gal-1 binding to glycosylated pre-B cell surface receptors. At the molecular and cellular levels, we identify α2,3-sialylated motifs as key targeted epitopes. This targeting occurs through a selectivity switch increasing Gal-1 contacts with α2,3-sialylated poly-N-acetyllactosamine upon pre-BCR interaction. Importantly, we observe that this switch is involved in the regulation of pre-BCR activation. Altogether, this study demonstrates that interactions to non-glycosylated proteins regulate the glycan-decoding functions of galectins at the cell surface.