Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers

Lakshminarayan, Ramya, Wunder, Christian, Becken, Ulrike, Howes, Mark T., Benzing, Carola, Arumugam, Senthil, Sales, Susanne, Ariotti, Nicholas, Chambon, Valérie, Lamaze, Christophe, Loew, Damarys, Shevchenko, Andrej, Gaus, Katharina, Parton, Robert G. and Johannes, Ludger (2014) Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers. Nature Cell Biology, 16 6: 592-603. doi:10.1038/ncb2970


Author Lakshminarayan, Ramya
Wunder, Christian
Becken, Ulrike
Howes, Mark T.
Benzing, Carola
Arumugam, Senthil
Sales, Susanne
Ariotti, Nicholas
Chambon, Valérie
Lamaze, Christophe
Loew, Damarys
Shevchenko, Andrej
Gaus, Katharina
Parton, Robert G.
Johannes, Ludger
Title Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers
Journal name Nature Cell Biology   Check publisher's open access policy
ISSN 1465-7392
1476-4679
Publication date 2014-01-01
Sub-type Article (original research)
DOI 10.1038/ncb2970
Open Access Status Not Open Access
Volume 16
Issue 6
Start page 592
End page 603
Total pages 12
Place of publication London, United Kingdom
Publisher Nature Publishing
Subject 1307 Cell Biology
Abstract Several cell surface molecules including signalling receptors are internalized by clathrin-independent endocytosis. How this process is initiated, how cargo proteins are sorted and membranes are bent remains unknown. Here, we found that a carbohydrate-binding protein, galectin-3 (Gal3), triggered the glycosphingolipid (GSL)-dependent biogenesis of a morphologically distinct class of endocytic structures, termed clathrin-independent carriers (CLICs). Super-resolution and reconstitution studies showed that Gal3 required GSLs for clustering and membrane bending. Gal3 interacted with a defined set of cargo proteins. Cellular uptake of the CLIC cargo CD44 was dependent on Gal3, GSLs and branched N-glycosylation. Endocytosis of Î 2 1-integrin was also reliant on Gal3. Analysis of different galectins revealed a distinct profile of cargoes and uptake structures, suggesting the existence of different CLIC populations. We conclude that Gal3 functionally integrates carbohydrate specificity on cargo proteins with the capacity of GSLs to drive clathrin-independent plasma membrane bending as a first step of CLIC biogenesis.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Institute for Molecular Bioscience - Publications
 
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