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Published 24 October 2005. doi:10.1083/jcb.200506026
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 2, 373-381
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Article

 Cell surface counter receptors are essential components of the unconventional export machinery of galectin-1

Claudia Seelenmeyer1, Sabine Wegehingel1, Ivo Tews1, Markus Künzler2, Markus Aebi2, and Walter Nickel1

1 Heidelberg University Biochemistry Center (BZH), 69120 Heidelberg, Germany
2 Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

Correspondence to walter.nickel{at}urz.uni-heidelberg.de

Galectin-1 is a component of the extracellular matrix as well as a ligand of cell surface counter receptors such as ß-galactoside–containing glycolipids, however, the molecular mechanism of galectin-1 secretion has remained elusive. Based on a nonbiased screen for galectin-1 export mutants we have identified 26 single amino acid changes that cause a defect of both export and binding to counter receptors. When wild-type galectin-1 was analyzed in CHO clone 13 cells, a mutant cell line incapable of expressing functional galectin-1 counter receptors, secretion was blocked. Intriguingly, we also find that a distant relative of galectin-1, the fungal lectin CGL-2, is a substrate for nonclassical export from Chinese hamster ovary (CHO) cells. Alike mammalian galectin-1, a CGL-2 mutant defective in ß-galactoside binding, does not get exported from CHO cells. We conclude that the ß-galactoside binding site represents the primary targeting motif of galectins defining a galectin export machinery that makes use of ß-galactoside–containing surface molecules as export receptors for intracellular galectin-1.

Claudia Seelenmeyer and Sabine Wegehingel contributed equally to this work.

Abbreviations used in this paper: APC, allophycocyanin; Gal-1, galectin-1.


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