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Published 9 May 2005. doi:10.1083/jcb.200407073
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 3, 491-501
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Article

 Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells

Delphine Delacour1, Valérie Gouyer1, Jean-Pierre Zanetta2, Hervé Drobecq3, Emmanuelle Leteurtre1, Georges Grard4, Odile Moreau-Hannedouche1, Emmanuel Maes2, Alexandre Pons2, Sabine André5, André Le Bivic6, Hans Joachim Gabius5, Aki Manninen7, Kai Simons7, and Guillemette Huet1

1 Unité INSERM 560, 59045 Lille Cedex, France
2 UMR CNRS 8576, Unité de Glycobiologie Structurale et Fonctionnelle, 59655 Villeneuve d'Ascq, France
3 UMR CNRS 8525, Institut de Biologie et Institut Pasteur de Lille, 59021 Lille, France
4 Laboratoire de Biochimie, Hôpital Claude Huriez, 59045 Lille Cedex, France
5 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, D-80539 Munchen, Germany
6 Laboratoire de Neurogenese et Morphogenese au cours du Developpement et chez l'Adulte (NMDA)/Institut de Biologie du Developpement de Marseille/IBDM, Case 907, Faculté des Sciences de Luminy, 13288 Marseille Cedex 09, France
7 Max-Planck Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany

Correspondence to Guillemette Huet: huet{at}lille.inserm.fr

We have previously reported that 1-benzyl-2-acetamido-2-deoxy-{alpha}-D-galactopyranoside (GalNAc{alpha}-O-bn), an inhibitor of glycosylation, perturbed apical biosynthetic trafficking in polarized HT-29 cells suggesting an involvement of a lectin-based mechanism. Here, we have identified galectin-4 as one of the major components of detergent-resistant membranes (DRMs) isolated from HT-29 5M12 cells. Galectin-4 was also found in post-Golgi carrier vesicles. The functional role of galectin-4 in polarized trafficking in HT-29 5M12 cells was studied by using a retrovirus-mediated RNA interference. In galectin-4–depleted HT-29 5M12 cells apical membrane markers accumulated intracellularly. In contrast, basolateral membrane markers were not affected. Moreover, galectin-4 depletion altered the DRM association characteristics of apical proteins. Sulfatides with long chain-hydroxylated fatty acids, which were also enriched in DRMs, were identified as high-affinity ligands for galectin-4. Together, our data propose that interaction between galectin-4 and sulfatides plays a functional role in the clustering of lipid rafts for apical delivery.

Abbreviations used in this paper: 2-D, 2-dimensional; AP, adaptor complex; CEA, carcinoembryonic antigen; CRD, carbohydrate recognition domain; DPP-IV, dipeptidylpeptidase-IV; DRM, detergent-resistant membrane; FAMEs, fatty-acid methyl esters; GalNAc{alpha}-O-bn, 1-benzyl-2-acetamido-2-deoxy-{alpha}-D-galactopyranoside; GC-MS, gas chromatography mass spectrometry; HPTLC, high performance thin layer chromatography; KD, knockdown; MALDI-TOF, matrix-assisted laser desorption/ionization–time of flight; RNAi, RNA interference; ST3Gal I, CMP-NeuAc: Galß1-3GalNAc {alpha}2,3-sialyltransferase.


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