Evidence map›Paper›PMID 24837829›Full record

ArticleNature cell biology2014

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

Ramya Lakshminarayan, Christian Wunder, Ulrike Becken, Mark T Howes, Carola Benzing, Senthil Arumugam, Susanne Sales, Nicholas Ariotti, Valérie Chambon, Christophe Lamaze and 5 more

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In one paragraph

Article in Nature cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed
10.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

167 citing papers in PubMed, 315 citations in OpenAlex.

  1. Encoding Cell-Surface Receptor Function Through Glycosylation: Lessons From CD44.Chembiochem : a European journal of chemical biology · 2026
    Review
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  14. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  15. Article
  16. Review
  17. Article
  18. The Historiography of Galactose and Its Recognition by Galectins.Advances in experimental medicine and biology · 2026
    Review
  19. Article
  20. Spatial N-glycan rearrangement on αNature communications · 2025
    Article

107 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 3 countries.

Ramya Lakshminarayan1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France [4] [5].
Christian Wunder1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France [4] [5].
Ulrike Becken1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France [4] [5].
Mark T HowesInstitute for Molecular Bioscience, University of Queensland, St Lucia, Queensland 4072, Australia.
Carola BenzingCentre for Vascular Research, Australian Centre for Nanomedicine and ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales, Sydney, New South Wales 2052, Australia.
Senthil Arumugam1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France.
Susanne SalesMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, 01307 Dresden, Germany.
Nicholas AriottiInstitute for Molecular Bioscience, University of Queensland, St Lucia, Queensland 4072, Australia.
Valérie Chambon1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France [4].
Christophe Lamaze1] CNRS UMR3666, 75005 Paris, France [2] INSERM U1143, 75005 Paris, France [3] Institut Curie-Centre de Recherche, Membrane Dynamics and Mechanics of Intracellular Signaling group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [4].
Damarys LoewInstitut Curie-Centre de Recherche, Proteomics and Mass Spectrometry Laboratory, 26 rue d'Ulm, 75248 Paris Cedex 05, France.
Andrej ShevchenkoMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, 01307 Dresden, Germany.
Katharina GausCentre for Vascular Research, Australian Centre for Nanomedicine and ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales, Sydney, New South Wales 2052, Australia.
Robert G PartonInstitute for Molecular Bioscience, University of Queensland, St Lucia, Queensland 4072, Australia.
Ludger Johannes1] Institut Curie-Centre de Recherche, Endocytic Trafficking and Therapeutic Delivery group, 26 rue d'Ulm, 75248 Paris Cedex 05, France [2] CNRS UMR3666, 75005 Paris, France [3] INSERM U1143, 75005 Paris, France [4].
Institut Curie · FRUniversity of Queensland · AUCentre National de la Recherche Scientifique · FRMax Planck Institute of Molecular Cell Biology and Genetics · DEUNSW Sydney · AUInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 β1-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.

Indexed as

EndocytosisAnimalsBlood ProteinsGalectin 3GalectinsGlycosphingolipidsGlycosylationHeLa CellsHumansHyaluronan ReceptorsIntegrin beta1MiceProtein Processing, Post-TranslationalProtein TransportRNA InterferenceTransfectionBlood ProteinsCD44 protein, humanCd44 protein, mouseGalectin 3GalectinsGlycosphingolipidsHyaluronan ReceptorsIntegrin beta1LGALS3 protein, human

Identifiers

PMID24837829
OpenAlexW2047109217

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.