%0 Journal Article
%A Berbís, M Álvaro
%A André, Sabine
%A Cañada, F Javier
%A Pipkorn, Rüdiger
%A Ippel, Hans
%A Mayo, Kevin H
%A Kübler, Dieter
%A Gabius, Hans-Joachim
%A Jiménez-Barbero, Jesús
%T Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner.
%J Biochemical and biophysical research communications
%V 443
%N 1
%@ 0006-291X
%C Orlando, Fla.
%I Academic Press
%M DKFZ-2017-00272
%P 126 - 131
%D 2014
%X 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.
%K Carbohydrates (NLM Chemicals)
%K Galectin 3 (NLM Chemicals)
%K Peptides (NLM Chemicals)
%K Recombinant Proteins (NLM Chemicals)
%K Tyrosine (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:24269589
%R 10.1016/j.bbrc.2013.11.063
%U https://inrepo02.dkfz.de/record/119641