@article {46424,
	title = {Hts/Adducin controls synaptic elaboration and elimination.},
	journal = {Neuron},
	volume = {69},
	year = {2011},
	month = {2011 Mar 24},
	pages = {1114-31},
	abstract = {<p>Neural development requires both synapse elaboration and elimination, yet relatively little is known about how these opposing activities are coordinated. Here, we provide evidence Hts/Adducin can serve this function. We show that Drosophila Hts/Adducin is enriched both pre- and postsynaptically at the NMJ. We then demonstrate that presynaptic Hts/Adducin is necessary and sufficient to control two opposing processes associated with synapse remodeling: (1) synapse stabilization as determined by light level and ultrastructural and electrophysiological assays and (2) the elaboration of actin-based, filopodia-like protrusions that drive synaptogenesis and growth. Synapse remodeling is sensitive to Hts/Adducin levels, and we provide evidence that the synaptic localization of Hts/Adducin is controlled via phosphorylation. Mechanistically, Drosophila Hts/Adducin protein has actin-capping activity. We propose that phosphorylation-dependent regulation of Hts/Adducin controls the level, localization, and activity of Hts/Adducin, influencing actin-based synapse elaboration and spectrin-based synapse stabilization. Hts/Adducin may define a mechanism to switch between synapse stability and dynamics.</p>
},
	keywords = {Actins, Animals, Animals, Genetically Modified, Biological Transport, Blotting, Western, Calmodulin-Binding Proteins, Cytoskeleton, Drosophila, Drosophila Proteins, Electrophysiology, Immunohistochemistry, Microscopy, Electron, Transmission, Phosphorylation, Spectrin, Synapses, Synaptic Transmission},
	issn = {1097-4199},
	doi = {10.1016/j.neuron.2011.02.007},
	author = {Pielage, Jan and Bulat, Victoria and Zuchero, J Bradley and Fetter, Richard D and Davis, Graeme W}
}
@article {46419,
	title = {A presynaptic giant ankyrin stabilizes the NMJ through regulation of presynaptic microtubules and transsynaptic cell adhesion.},
	journal = {Neuron},
	volume = {58},
	year = {2008},
	month = {2008 Apr 24},
	pages = {195-209},
	abstract = {<p>In a forward genetic screen for mutations that destabilize the neuromuscular junction, we identified a novel long isoform of Drosophila ankyrin2 (ank2-L). We demonstrate that loss of presynaptic Ank2-L not only causes synapse disassembly and retraction but also disrupts neuronal excitability and NMJ morphology. We provide genetic evidence that ank2-L is necessary to generate the membrane constrictions that normally separate individual synaptic boutons and is necessary to achieve the normal spacing of subsynaptic protein domains, including the normal organization of synaptic cell adhesion molecules. Mechanistically, synapse organization is correlated with a lattice-like organization of Ank2-L, visualized using extended high-resolution structured-illumination microscopy. The stabilizing functions of Ank2-L can be mapped to the extended C-terminal domain that we demonstrate can directly bind and organize synaptic microtubules. We propose that a presynaptic Ank2-L lattice links synaptic membrane proteins and spectrin to the underlying microtubule cytoskeleton to organize and stabilize the presynaptic terminal.</p>
},
	keywords = {Amino Acid Motifs, Animals, Animals, Genetically Modified, Ankyrins, Cell Adhesion Molecules, Neuronal, Drosophila, Drosophila Proteins, Gene Expression Regulation, Horseradish Peroxidase, Larva, Luminescent Proteins, Microscopy, Electron, Transmission, Microtubules, Mutation, Neuromuscular Junction, Presynaptic Terminals, Synapsins, Synaptic Transmission},
	issn = {1097-4199},
	doi = {10.1016/j.neuron.2008.02.017},
	author = {Pielage, Jan and Cheng, Ling and Fetter, Richard D and Carlton, Pete M and Sedat, John W and Davis, Graeme W}
}
