Glycogen Synthase Kinase 3

Supporting information

Glycogen synthase kinase 3 (GSK-3), a serine-threonine kinase with two isoforms (α and β), was originally discovered as a key enzyme in glycogen metabolism. GSK-3 was subsequently shown to function in cell division, proliferation, motility and survival. GSK-3 plays a role in a number of pathological conditions including cancer and diabetes and is increasingly seen as an important component of neurological diseases.

GSK-3 phosphorylates tau and presenilin-1, which are involved in the development of Alzheimer's disease. Both isoforms of GSK-3 are ubiquitously expressed, although particularly high levels of GSK-3β are found in the brain where it is involved in synaptic plasticity, possibly via regulation of NMDA receptor trafficking. GSK-3 phosphorylates over 40 different substrates including signaling proteins, transcription factors and structural proteins, and is part of the signal transduction cascade of a large number of growth factors and cytokines. The activity of GSK is regulated by phosphorylation (Akt, S6K, RSK, PKA and PKC), dephosphorylation (PP1 and PP2A), and by binding to protein complexes (with β-catenin, axin, CK1 and the APC complex).

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
GSK-3α Human GSK3A NM_019884 P49840
Mouse Gsk3a NM_001031667 Q2NL51
Rat Gsk3a NM_017344 P18265
GSK-3β Human GSK3B NM_002093 P49841
Mouse Gsk3b NM_019827 Q9WV60
Rat Gsk3b NM_032080 P18266

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