NDLI: CASK and CaMKII function in the mushroom body α′/β′ neurons during Drosophila memory formation

Content Provider	PubMed Central
Author	Malik, Bilal R. Gillespie, John Michael Hodge, James J. L.
Copyright Year	2013
Abstract	Ca2+/CaM serine/threonine kinase II (CaMKII) is a central molecule in mechanisms of synaptic plasticity and memory. A vital feature of CaMKII in plasticity is its ability to switch to a calcium (Ca2+) independent constitutively active state after autophosphorylation at threonine 287 (T287). A second pair of sites, T306 T307 in the calmodulin (CaM) binding region once autophosphorylated, prevent subsequent CaM binding and inactivates the kinase during synaptic plasticity and memory. Recently a synaptic molecule called Ca2+/CaM-dependent serine protein kinase (CASK) has been shown to control both sets of CaMKII autophosphorylation events and hence is well poised to be a key regulator of memory. We show deletion of full length CASK or just its CaMK-like and L27 domains disrupts middle-term memory (MTM) and long-term memory (LTM), with CASK function in the α′/β′ subset of mushroom body neurons being required for memory. Likewise directly changing the levels of CaMKII autophosphorylation in these neurons removed MTM and LTM. The requirement of CASK and CaMKII autophosphorylation was not developmental as their manipulation just in the adult α′/β′ neurons was sufficient to remove memory. Overexpression of CASK or CaMKII in the α′/β′ neurons also occluded MTM and LTM. Overexpression of either Drosophila or human CASK in the α′/β′ neurons of the CASK mutant completely rescued memory, confirming that CASK signaling in α′/β′ neurons is necessary and sufficient for Drosophila memory formation and that the neuronal function of CASK is conserved between Drosophila and human. At the cellular level CaMKII overexpression in the α′/β′ neurons increased activity dependent Ca2+ responses while reduction of CaMKII decreased it. Likewise reducing CASK or directly expressing a phosphomimetic CaMKII T287D transgene in the α′/β′ similarly decreased Ca2+ signaling. Our results are consistent with CASK regulating CaMKII autophosphorylation in a pathway required for memory formation that involves activity dependent changes in Ca2+ signaling in the α′/β′ neurons.
Related Links	http://dx.doi.org/10.3389/fncir.2013.00052
Starting Page	52
File Format	PDF
ISSN	16625110
e-ISSN	16625110
Journal	Frontiers in Neural Circuits
Volume Number	7
Language	English
Publisher	Frontiers Media S.A.
Publisher Date	2013-01-01
Access Restriction	Open
Rights Holder	Frontiers Media S.A.
Subject Keyword	Sensory Systems Cognitive Neuroscience Cellular and Molecular Neuroscience Neuroscience (miscellaneous) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cognitive Neuroscience Sensory Systems Cellular and Molecular Neuroscience

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