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The bitopic membrane glycoproteins of the integrin family adopt different conformations when altering between active and inactive states. Their multiple glycans then alter their spatial configuration, which can encode for specific function, notably their endocytic fate. The oligomerization-competent galectin-3 binds to the terminal galactose moieties of complex glycans. Only on a compact bent-closed conformation of integrin, galectin-binding glycosylation sites are in close spatial proximity such that oligomerization of galectin-3 is possible and ultimately results in membrane invaginations, leading to clathrin-independent glycolipid-lectin-driven endocytosis. We strive to reveal the molecular mechanisms underlying galectin binding, oligomerization, and glycan dependence thereof. Recently, we visualized galectin-3 oligomoers up to tetramers bound to particular glycans on α5β1 integrin (Shafaq-Zadah M. et al., Nat. Commun, 2025).
The Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) is part of the Forschungsverbund Berlin e.V. (FVB), which legally represents seven non-university research institutes - members of the Leibniz Association - in Berlin.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Rudower Chaussee 17
12489 Berlin, Germany
