Affiliations: Instituto de Investigaciones Biomédicas,
Consejo Superior de Investigaciones Científicas and Universidad
Autónoma de Madrid, c/ Arturo Duperier 4, E-28029 Madrid, Spain
Note: [] Address for correspondence: A. Villalobo Instituto de
Investigaciones Biomédicas Consejo Superior de Investigaciones
Científicas and Universidad Autónoma de Madrid c/ Arturo
Duperier 4 E-28029 Madrid, Spain. e-mail: antonio.villalobo@iib.uam.es Tel: 91
585 4600 FAX: 91 585 4587
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.
Keywords: Cellular signaling, lectins, protein glycosylation, protein phosphorylation