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The enzyme was first isolated and purified as an activity capable of phosphorylating and inhibiting glycogen synthase. Glycogen synthase kinase-3 is an evolutionary conserved, ubiquitous serine/threonine protein kinase, belonging to the CMCG family of the proline-directed kinases ( C yclin-dependent kinases ( C DKs), M itogen-activated protein kinases ( M APKs), G lycogen synthase kinases ( G SKs), and C DK-like kinases ( C LKs)). Taken together, these data support a role for the GSK-3α gene in CNS functioning and possible involvement in the development of psychiatric disorders. Changes in cerebellar structure and function were observed in mutant mice along with a significant decrease of the number and size of Purkinje cells. GSK-3α KO mice exhibited a deficit in fear conditioning, however memory formation as assessed by a passive avoidance test was normal, suggesting that the animals are sensitized for active avoidance of a highly aversive stimulus in the fear-conditioning paradigm.

However, genetic inactivation of the GSK-3α gene was associated with: decreased locomotion and impaired motor coordination, increased grooming activity, loss of social motivation and novelty enhanced sensorimotor gating and impaired associated memory and coordination. Similar to the previously described behaviours of GSK-3β +/-mice, GSK-3α mutants display decreased exploratory activity, decreased immobility time and reduced aggressive behavior. In this study, we have characterized brain functions of GSK-3α KO mice by using a well-established battery of behavioral tests together with neurochemical and neuroanatomical analysis. Mice lacking a functional GSK-3α gene were engineered in our laboratory they are viable and display insulin sensitivity. Glycogen synthase kinase-3 (GSK-3) is a widely expressed and highly conserved serine/threonine protein kinase encoded by two genes that generate two related proteins: GSK-3α and GSK-3β.

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