Phosphorylated human galectin-3: Facile large-scale preparation of active lectin and detection of structural changes by CD spectroscopy

Kübler, Dieter; Hung, Chien Wen; Dam, Tarun K.; Kopitz, Jürgen; André, Sabine; Kaltner, Herbert; Lohr, Michaela; Manning, Joachim C.; He, Lizhong; Wang, Hui; Middelberg, Anton P. J.; Brewer, C. Fred; Reed, Jennifer; Lehmann, Wolf D.; Gabius, Hans‐Joachim

doi:10.1016/j.bbagen.2008.01.018

Cited by 37 publications

(40 citation statements)

References 27 publications

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“…Proteolytic truncation by collagenase, phosphorylation by casein kinase 1, and biotinylation were carried out with quality controls and activity assays by solid-phase and cell binding as described previously Kübler et al, 2008) (supplementary material Fig. S1).…”

Section: Methodsmentioning

confidence: 99%

“…Owing to its trimodular design the chimera-type galectin-3 (Gal-3) is unique within this family. In addition to its carbohydrate recognition domain, it harbours a collagenase-sensitive stalk, instrumental for pentamerization in the presence of multivalent ligands (Ahmad et al, 2004), and an N-terminal sequence with sites for casein-kinase-1-dependent serine phosphorylation (Cowles et al, 1990;Huflejt et al, 1993;Kübler et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…In order to further probe into its functional relevance we previously developed an efficient strategy to produce phosphorylated Gal-3 (pGal-3) in large quantities (Kübler et al, 2008). This procedure has made it possible to monitor carbohydrate and cell binding comparatively (Kübler et al, 2008;Szabo et al, 2009) and is a prerequisite for detailed functional studies. Having also previously initiated the monitoring of the involvement of galectins in axonal development with two prototype chicken galectins (Kopitz et al, 2004), the access to pGal-3 allows us to address the issue of the functional relevance of Gal-3 phosphorylation in this respect.…”

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of adhesion- and growth-regulatory human galectin-3 leads to the induction of axonal branching by local membrane L1 and ERM redistribution

Díez-Revuelta

Velasco

André

et al. 2010

Journal of Cell Science

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SummarySerine phosphorylation of the -galactoside-binding protein galectin-3 (Gal-3) impacts nuclear localization but has unknown consequences for extracellular activities. Herein, we reveal that the phosphorylated form of galectin-3 (pGal-3), adsorbed to substratum surfaces or to heparan sulphate proteoglycans, is instrumental in promoting axon branching in cultured hippocampal neurons by local actin destabilization. pGal-3 interacts with neural cell adhesion molecule L1, and enhances L1 association with Thy-1-rich membrane microdomains. Concomitantly, membrane-actin linker proteins ezrin-radixin-moesin (ERM) are recruited to the same membrane site via interaction with the intracellular domain of L1. We propose that the local regulation of the L1-ERM-actin pathway, at the level of the plasma membrane, underlies pGal-3-induced axon branching, and that galectin phosphorylation in situ could act as a molecular switch for the axon response to Gal-3.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of adhesion- and growth-regulatory human galectin-3 leads to the induction of axonal branching by local membrane L1 and ERM redistribution

Díez-Revuelta

Velasco

André

et al. 2010

Journal of Cell Science

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“…Galectin-3 consists of three parts: 1) a N-terminal 12 amino acid leader sequence containing two phosphorylation sites, 2) a proline and glycine rich collagen like domain necessary for oligomerisation and 3) the carbohydrate recognition domain (Ahmad et al, 2004a;Dumic et al, 2006;Kubler et al, 2008;Mehul & Hughes, 1997;Nieminen et al, 2008). The first few amino acids forming the leader peptide are important for the subcellular localisation and secretion of the protein (Gong et al, 1999).…”

Section: Galectin-3: the Only Known Chimera Type Galectinmentioning

confidence: 99%

Galectins: Structures, Binding Properties and Function in Cell Adhesion

Römer¹,

Elling²

2011

Biomaterials - Physics and Chemistry

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Toward Comprehensive Analysis of the Galectin Network in Chicken: Unique Diversity of Galectin‐3 and Comparison of its Localization Profile in Organs of Adult Animals to the Other Four Members of this Lectin Family

Kaltner

Kübler

López‐Merino

et al. 2011

The Anatomical Record

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Characterization of all members of a gene family established by gene divergence is essential to delineate distinct or overlapping expression profiles and functionalities. Their activity as potent modulators of diverse physiological processes directs interest to galectins (endogenous lectins with b-sandwich fold binding b-galactosides and peptide motifs), warranting their study with the long-term aim of a comprehensive analysis. The comparatively low level of complexity of the galectin network in chicken with five members explains the choice of this organism as model. Previously, the three proto-type chicken galectins CG-1A, CG-1B, and CG-2 as well as the tandem-repeat-type CG-8 had been analyzed. Our study fills the remaining gap to determine gene structure, protein characteristics and expression profile of the fifth protein, that is, chimera-type chicken galectin-3 (CG-3). Its gene has a unique potential to generate variants: mRNA production stems from two promoters, alternative splicing of the form from the second transcription start point (tsp) can generate three mRNAs. The protein with functional phosphorylation sites in the N-terminus generated by transcription from the first tsp (tsp1CG-3) is the predominant CG-3 type present in adult tissues. Binding assays with neoglycoproteins and cultured cells disclose marked similarity to properties of human galectin-3. The expression and localization profiles as well as proximal promoter regions have characteristic features distinct from the other four CGs. This information on CG-3 completes the description

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Phosphorylated human galectin-3: Facile large-scale preparation of active lectin and detection of structural changes by CD spectroscopy

Cited by 37 publications

References 27 publications

Phosphorylation of adhesion- and growth-regulatory human galectin-3 leads to the induction of axonal branching by local membrane L1 and ERM redistribution

Phosphorylation of adhesion- and growth-regulatory human galectin-3 leads to the induction of axonal branching by local membrane L1 and ERM redistribution

Galectins: Structures, Binding Properties and Function in Cell Adhesion

Toward Comprehensive Analysis of the Galectin Network in Chicken: Unique Diversity of Galectin‐3 and Comparison of its Localization Profile in Organs of Adult Animals to the Other Four Members of this Lectin Family

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