Akt regulates glutamate receptor trafficking and postsynaptic membrane elaboration at theDrosophilaneuromuscular junction

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The Akt family of serine-threonine kinases integrates a myriad of signals governing cell proliferation, apoptosis, glucose metabolism, and cytoskeletal organization. Akt affects neuronal morphology and function, influencing dendrite growth and the expression of ion channels. Akt is also an integral element of PI3Kinase-target of rapamycin (TOR)-Rheb signaling, a pathway that affects synapse assembly in both vertebrates andDrosophila. Our recent findings demonstrated that disruption of this pathway inDrosophilais responsible for a number of neurodevelopmental deficits that may also affect phenotypes associated with tuberous sclerosis complex, a disorder resulting from mutations compromising the TSC1/TSC2 complex, an inhibitor of TOR (Dimitroff et al., 2012). Therefore, we examined the role of Akt in the assembly and physiological function of theDrosophilaneuromuscular junction (NMJ), a glutamatergic synapse that displays developmental and activity-dependent plasticity. The singleDrosophila Aktfamily member,Akt1selectively altered the postsynaptic targeting of one glutamate receptor subunit, GluRIIA, and was required for the expansion of a specialized postsynaptic membrane compartment, the subsynaptic reticulum (SSR). Several lines of evidence indicated thatAkt1influences SSR assembly by regulation of Gtaxin, aDrosophilat-SNARE protein (Gorczyca et al., 2007) in a manner independent of the mislocalization of GluRIIA. Our findings show thatAkt1governs two critical elements of synapse development, neurotransmitter receptor localization, and postsynaptic membrane elaboration.

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