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Biochem Biophys Res Commun. 2014 Jan 3;443(1):126-31. doi: 10.1016/j.bbrc.2013.11.063. Epub 2013 Nov 22.

Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner.

Author information

  • 1Chemical and Physical Biology Department, Centro de Investigaciones Biológicas, CSIC, 28040 Madrid, Spain.
  • 2Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians University, 80539 Munich, Germany.
  • 3Central Peptide Synthesis Unit, German Cancer Research Center, 69120 Heidelberg, Germany.
  • 4Department of Biochemistry, CARIM, University of Maastricht, Maastricht, The Netherlands; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • 5Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
  • 6Biomolecular Interactions, German Cancer Research Center, 69120 Heidelberg, Germany.
  • 7Chemical and Physical Biology Department, Centro de Investigaciones Biológicas, CSIC, 28040 Madrid, Spain. Electronic address: jjbarbero@cib.csic.es.

Abstract

Galectin-3 (Gal-3) is a multi-functional effector protein that functions in the cytoplasm and the nucleus, as well as extracellularly following non-classical secretion. Structurally, Gal-3 is unique among galectins with its carbohydrate recognition domain (CRD) attached to a rather long N-terminal tail composed mostly of collagen-like repeats (nine in the human protein) and terminating in a short non-collagenous terminal peptide sequence unique in this lectin family and not yet fully explored. Although several Ser and Tyr sites within the N-terminal tail can be phosphorylated, the physiological significance of this post-translational modification remains unclear. Here, we used a series of synthetic (phospho)peptides derived from the tail to assess phosphorylation-mediated interactions with (15)N-labeled Gal-3 CRD. HSQC-derived chemical shift perturbations revealed selective interactions at the backface of the CRD that were attenuated by phosphorylation of Tyr 107 and Tyr 118, while phosphorylation of Ser 6 and Ser 12 was essential. Controls with sequence scrambling underscored inherent specificity. Our studies shed light on how phosphorylation of the N-terminal tail may impact on Gal-3 function and prompt further studies using phosphorylated full-length protein.

Copyright © 2013 Elsevier Inc. All rights reserved.

KEYWORDS:

Agglutinin; CRD; Collagen; Gal-3; HSQC; Lectin; NMR; Phosphopeptide; Phosphorylation; carbohydrate recognition domain; galectin-3; heteronuclear single-quantum coherence; nuclear magnetic resonance

PMID:
24269589
[PubMed - indexed for MEDLINE]
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