Glycogen synthase kinase-3 (GSK3), a multifunctional serine/threonine kinase, is a key regulator of a number of signaling pathways. Two GSK3 paralogs have been described in mammals: GSK3α and GSK3β, which are 85% homologous to each other and exhibit about 98% homology in the kinase domains and consequently, a high structural similarity. However, some functional differences between both paralogs have been reported. In this work, we review the similarities and differences between GSK3α and GSK3β proteins in relation with their structure and function.
Keywords: GSK3 paralog, polyglycine repeats, kinase inhibitors, glycogen synthase kinases, N- and C-termini, inflammatory response, GSK3 1 phosphorylates phospho-glycogen synthase2 peptide, KESTREL, GSK3, Arg180, Cys205, ATP-binding sites, Dyctiostelium discoidium -catenin, tissue-specific expression, extracellular signals
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