Journal
JOURNAL OF CELL BIOLOGY
Volume 204, Issue 1, Pages 77-94Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201305134
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Funding
- Swiss National Science Foundation
- Friedrich Miescher Institute for Biomedical Research
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The precise regulation of synapse maintenance is critical to the development and function of neuronal circuits. Using an in vivo RNAi screen targeting the Drosophila kinome and phosphatome, we identify 11 kinases and phosphatases controlling synapse stability by regulating cytoskeletal, phospholipid, or metabolic signaling. We focus on casein kinase 2 (CK2) and demonstrate that the regulatory (beta) and catalytic (alpha) subunits of CK2 are essential for synapse maintenance. CK2 alpha kinase activity is required in the presynaptic motoneuron, and its interaction with CK2 beta, mediated cooperatively by two N-terminal residues of CK2 alpha, is essential for CK2 holoenzyme complex stability and function in vivo. Using genetic and biochemical approaches we identify Ankyrin2 as a key presynaptic target of CK2 to maintain synapse stability. In addition, CK2 activity controls the subcellular organization of individual synaptic release sites within the presynaptic nerve terminal. Our study identifies phosphorylation of structural synaptic components as a compelling mechanism to actively control the development and longevity of synaptic connections.
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