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TitleSpatial N-glycan rearrangement on αβ integrin nucleates galectin-3 oligomers to determine endocytic fate.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9461, Year 2025
Publish dateOct 27, 2025
AuthorsMassiullah Shafaq-Zadah / Estelle Dransart / Ilyes Hamitouche / Christian Wunder / Valérie Chambon / Cesar A Valades-Cruz / Ludovic Leconte / Nirod Kumar Sarangi / Jack Robinson / Siau-Kun Bai / Raju Regmi / Aurélie Di Cicco / Agnès Hovasse / Richard Bartels / Ulf J Nilsson / Sarah Cianférani-Sanglier / Hakon Leffler / Tia E Keyes / Daniel Lévy / Stefan Raunser / Daniel Roderer / Ludger Johannes /
PubMed AbstractMembrane glycoproteins frequently adopt different conformations when altering between active and inactive states. Here, we discover a molecular switch that exploits dynamic spatial rearrangements of ...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 αβ integrin, we find that only the bent-closed state arranges N-glycans to nucleate the formation of up to tetrameric oligomers of the glycan-binding protein galectin-3. We propose a structural model of how these galectin-3 oligomers are built and how they clamp the bent-closed state to select it for endocytic uptake and subsequent retrograde trafficking to the Golgi for polarized distribution in cells. Our findings reveal the dynamic regulation of the glycan landscape at the cell surface to achieve oligomerization of galectin-3. Galectin-3 oligomers are thereby identified as functional decoders of defined spatial patterns of N-glycans on specifically the bent-closed conformational state of αβ integrin and possibly other integrin family members.
External linksNat Commun / PubMed:41145507 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 8.5 Å
Structure data

17269

8oxz

EMDB-17269, PDB-8oxz:
Rat alpha5beta1 integrin, headpiece
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-17270: Rat alpha5beta1 integrin, leg piece
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-51027: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 dimer
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-51028: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 trimer
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-51029: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 tetramer
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-54200: Complex of peptidisc-embedded alpha5beta1 integrin and galectin-3
Method: EM (single particle) / Resolution: 6.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • rattus norvegicus (Norway rat)
  • Homo sapiens (human)
KeywordsCELL ADHESION / integrin / glycoprotein / membrane protein

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