Proteomics

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Dynamic N-glycan rearrangement nucleates galectin-3 oligomers and drives endocytosis

ABSTRACT: Membrane glycoproteins often adopt different conformations when shifting between active and inactive states. Here, we discover a molecular switch that operates through major changes in the spatial arrangement of the N-glycan landscape during such conformational transitions. We demonstrate that the cell adhesion glycoprotein alpha5 beta1 integrin selectively in its bent-closed inactive conformational state nucleates the formation of ring-shaped tetramers of the glycan-binding protein galectin-3 to drive endocytic uptake. We propose a novel structural model to explain how spatial rearrangement of N-glycans transduced by conformational changes results in galectin-3 tetramers. Our findings identify local arrangements of N-glycans as unexpectedly dynamic regulatory elements at the cell surface and provide a new facet to higher order pattern interactions with glycoproteins for regulation of processes such as galectin-dependent endocytosis.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human)

SUBMITTER: Agnès Hovasse  

LAB HEAD: Agnes Hovasse

PROVIDER: PXD041522 | Pride | 2025-11-10

REPOSITORIES: Pride

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Publications

Membrane glycoproteins frequently adopt different conformations when altering between active and inactive states. Here, we discover a molecular switch that exploits dynamic spatial rearrangements of N-glycans during such conformational transitions to control protein function. For the conformationally switchable cell adhesion glycoprotein α<sub>5</sub>β<sub>1</sub> integrin, we find that only the bent-closed state arranges N-glycans to nucleate the formation of up to tetrameric oligomers of the g  ...[more]

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