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Significance Neuromodulation is pivotal for brain function. One of the key pathways engaged by neuromodulators is signaling via second messenger cAMP, which controls a myriad of fundamental reactions. This study identifies KCTD5, a ubiquitin ligase adapter, as a regulatory element in this pathway and determines that it works by an unusual dual mode controlling the activity of cAMP-generating enzyme in neurons through both zinc transport and G protein signaling.
Muntean et al. (Tue,) studied this question.
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