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-Structure paper
| タイトル | Spatial N-glycan rearrangement on αβ integrin nucleates galectin-3 oligomers to determine endocytic fate. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 9461, Year 2025 |
| 掲載日 | 2025年10月27日 |
著者 | Massiullah 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 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:41145507 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.7 - 8.5 Å |
| 構造データ | EMDB-17269, PDB-8oxz: ![]() EMDB-17270: Rat alpha5beta1 integrin, leg piece ![]() EMDB-51027: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 dimer ![]() EMDB-51028: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 trimer ![]() EMDB-51029: Complex of nanodisc-embedded alpha5beta1 integrin with Gal3 tetramer ![]() EMDB-54200: Complex of peptidisc-embedded alpha5beta1 integrin and galectin-3 |
| 化合物 | ![]() ChemComp-NAG: |
| 由来 |
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キーワード | CELL ADHESION / integrin / glycoprotein / membrane protein |
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Homo sapiens (ヒト)
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