RRC ID 32488
Author Bulat V, Rast M, Pielage J.
Title Presynaptic CK2 promotes synapse organization and stability by targeting Ankyrin2.
Journal J Cell Biol
Abstract 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 (β) and catalytic (α) subunits of CK2 are essential for synapse maintenance. CK2α kinase activity is required in the presynaptic motoneuron, and its interaction with CK2β, mediated cooperatively by two N-terminal residues of CK2α, 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.
Volume 204(1)
Pages 77-94
Published 2014-1-6
DOI 10.1083/jcb.201305134
PII jcb.201305134
PMID 24395637
PMC PMC3882785
MeSH Animals Ankyrins / metabolism* Casein Kinase II / metabolism* Cytoskeleton / metabolism Drosophila Drosophila Proteins / metabolism* Phospholipids / metabolism Phosphoric Monoester Hydrolases / metabolism Phosphorylation Signal Transduction / physiology Synapses / metabolism Synapses / physiology*
IF 8.811
Times Cited 16
Drosophila DGRC#141869 DGRC#141994