Abstract
The posttranslational N- and O-glycosylation of proteins and the recognition of their glycosylated moieties by endogenous lectins play important physiological roles in animal cells. These processes are ubiquitous in the animal kingdom, and have been observed from the lowest nematode to man. After a lectin specifically recognizes a glycoligand, the cellular machinery transfers that information to their different targets to attain specific cellular responses through a network of signaling pathways. In this short assay, the involvement of lectins in signaling processes, the modification of the binding activity of lectins by precise signaling systems, and the possible role of lectins recognizing O-glycosylated intracellular proteins as recruitment sites to initiate new signaling events, will be discussed.
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