TY  - JOUR
AU  - Berbís, M Álvaro
AU  - André, Sabine
AU  - Cañada, F Javier
AU  - Pipkorn, Rüdiger
AU  - Ippel, Hans
AU  - Mayo, Kevin H
AU  - Kübler, Dieter
AU  - Gabius, Hans-Joachim
AU  - Jiménez-Barbero, Jesús
TI  - Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner.
JO  - Biochemical and biophysical research communications
VL  - 443
IS  - 1
SN  - 0006-291X
CY  - Orlando, Fla.
PB  - Academic Press
M1  - DKFZ-2017-00272
SP  - 126 - 131
PY  - 2014
AB  - 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.
KW  - Carbohydrates (NLM Chemicals)
KW  - Galectin 3 (NLM Chemicals)
KW  - Peptides (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - Tyrosine (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:24269589
DO  - DOI:10.1016/j.bbrc.2013.11.063
UR  - https://inrepo02.dkfz.de/record/119641
ER  -