Phosphorylation of multifunctional galectins by protein kinases CK1, CK2, and PKA

摘要: Phosphorylation is known to have a strong impact on protein functions. We analyzed members of the lectin family multifunctional galectins as targets kinases CK1, CK2, and PKA. Galectins are potent growth regulators able bind both glycan peptide motifs at intra- extracellular sites. Performing in vitro kinase assays, galectin phosphorylation was detected by phosphoprotein staining autoradiography. The insertion phosphoryl groups varied large extent depending type applied respective substrate. Sites observed recombinant were determined strategic combination phosphopeptide enrichment nano-ultra-performance liquid chromatography tandem mass spectrometry (nanoUPLC–MS/MS). By silico modeling, sites visualized three-dimensionally. Our results reveal galectin-type-specific Ser-/Thr-dependent beyond example galectin-3. These data basis for functional studies also illustrate analytical sensitivity methods further work human lectins.