Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells

Patnaik, Santosh K.; Potvin, Barry; Carlsson, Susanne; Sturm, David J.; Leffler, Hakon; Stanley, Pamela

doi:10.1093/glycob/cwj063

Cited by 131 publications

(119 citation statements)

References 85 publications

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“…Galectin-3 binds to galactose, a terminal residue that might be exposed at the carbohydrate chain termini of the mature complex N-glycans (69). Consistently, the efficiency of coimmunoprecipitation of gp114 with galectin-3 and formation of the high-molecular-weight clusters containing gp114 and galectin-3, as well as apical distribution of gp114 are severely impaired in galactosylation-deficient MDCKII-RCAr cells (15,17,48).…”

Section: Reviewmentioning

confidence: 76%

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Vagin

Kraut²,

Sachs³

2009

American Journal of Physiology-Renal Physiology

177

157

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ized distribution of plasma membrane transporters and receptors in epithelia is essential for vectorial functions of epithelia. This polarity is maintained by sorting of membrane proteins into apical or basolateral transport containers in the transGolgi network and/or endosomes followed by their delivery to the appropriate plasma membrane domains. Sorting depends on the recognition of sorting signals in proteins by specific sorting machinery. In the present review, we summarize experimental evidence for and against the hypothesis that N-glycans attached to the membrane proteins can act as apical sorting signals. Furthermore, we discuss the roles of N-glycans in the apical sorting event per se and their contribution to folding and quality control of glycoproteins in the endoplasmic reticulum or retention of glycoproteins in the plasma membrane. Finally, we review existing hypotheses on the mechanism of apical sorting and discuss the potential roles of the lectins, VIP36 and galectin-3, as putative apical sorting receptors. apical sorting; apical membrane retention; H-K-ATPase ␤-subunit; lectin EPITHELIAL CELLS CARRY OUT vectorial transport that requires polarized distribution of transporters and receptors to apical or basolateral membrane domains. These domains are separated by tight junctions that connect neighboring cells in the epithelial monolayer and act as diffusion barriers to prevent mixing of apical and basolateral membrane components (22). Asymmetric distribution of plasma membrane proteins is accomplished by their sorting into apical and basolateral containers in the trans-Golgi network (TGN) and/or endosomes followed by vectorial transport of these containers and insertion and retention of the proteins in the appropriate plasma membrane domains. Sorting depends on recognition of apical and basolateral sorting signals within the proteins by cellular sorting machinery (20,58,59,75,76).Numerous studies have indicated that both O-and N-glycans attached to the extracellular domains of some membrane proteins are important for apical location of these proteins. This review will focus on the role of N-glycans in polarized distribution of plasma membrane proteins in epithelia. The role of O-glycans in apical sorting has been described in several recent excellent reviews (18, 71) and will not be discussed further here.A putative role of N-glycans as apical sorting signals was postulated more than 10 years ago (24, 31). However, this hypothesis remains controversial primarily because N-glycans are important for the processes that precede or follow the actual sorting event, such as protein folding, quality control, endoplasmic reticulum (ER)-associated degradation, ER-to-Golgi trafficking, and retention of glycoproteins in the apical membrane. Therefore, merely examining the effect of altering the number or the nature of N-linked glycans on the relative abundance of the glycoprotein in the apical membrane, as has been done in many of the studies reported, does not allow one to distinguish between effects on apica...

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Section: Reviewmentioning

confidence: 76%

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Vagin

Kraut²,

Sachs³

2009

American Journal of Physiology-Renal Physiology

177

157

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“…Galectins preferentially bind β-galactoside-containing glycans comprised of repeating units of N-acetyllactosamine (Galβ1,4GlcNAc; LacNAc), either as disaccharide units at the termini of complex N-glycans, or as repeating units in a poly-N-acetyllactosamine chain on N-or O-glycans [5,7,8]. Galectin binding affinities to complex N-glycans are proportional to their LacNAc content and to their GlcNAc branching [5,[7][8][9][10][11].…”

Section: Biochemical Aspects Of Galectin-glycoprotein Lattices Formationmentioning

confidence: 99%

Functions of cell surface galectin-glycoprotein lattices

Rabinovich

Toscano

Jackson

et al. 2007

Current Opinion in Structural Biology

358

318

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Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases, can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for β-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions and immune cell activation and homeostasis.

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“…One family of multivalent lectins that can organize cell surface lattices is the galectins 7 . Galectins preferentially bind b-galactoside-containing glycans comprised of repeating units at the termini of complex N-glycans or as repeating units in a poly-N-acetyllactosamine chain on N-glycan or O-glycan [7][8][9] . The galectins share a common carbohydrate recognition domain (CRD) responsible for b-galactoside binding 10 and have been shown to be involved in cell interactions, proliferation, migration, apoptosis and mRNA splicing 3,[11][12][13] .…”

mentioning

confidence: 99%

Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

et al. 2015

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Galectins are glycan-binding proteins involved in various biological processes including cell/cell interactions. During B-cell development, bone marrow stromal cells secreting galectin-1 (GAL1) constitute a specific niche for pre-BII cells. Besides binding glycans, GAL1 is also a pre-B cell receptor (pre-BCR) ligand that induces receptor clustering, the first checkpoint of B-cell differentiation. The GAL1/pre-BCR interaction is the first example of a GAL1/unglycosylated protein interaction in the extracellular compartment. Here we show that GAL1/pre-BCR interaction modifies GAL1/glycan affinity and particularly inhibits binding to LacNAc containing epitopes. GAL1/pre-BCR interaction induces local conformational changes in the GAL1 carbohydrate-binding site generating a reduction in GAL1/glycan affinity. This fine tuning of GAL1/glycan interactions may be a strategic mechanism for allowing pre-BCR clustering and pre-BII cells departure from their niche. Altogether, our data suggest a novel mechanism for a cell to modify the equilibrium of the GAL1/glycan lattice involving GAL1/unglycosylated protein interactions.

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Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells

Cited by 131 publications

References 85 publications

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Functions of cell surface galectin-glycoprotein lattices

Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

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