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The Journal of Neuroscience, January 12, 2005, 25(2):479-487; doi:10.1523/JNEUROSCI.2699-04.2005

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Cellular/Molecular
Postsynaptic Shank Antagonizes Dendrite Branching Induced by the Leucine-Rich Repeat Protein Densin-180

Arne Quitsch, Kerstin Berhörster, Chong Wee Liew, Dietmar Richter, and Hans-Jürgen Kreienkamp

Institut für Zellbiochemie und klinische Neurobiologie, Universitätskrankenhaus Hamburg-Eppendorf, 20246 Hamburg, Germany

Leucine-rich repeat and PDZ [postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1] domain proteins such as scribble and Densin-180 have been implicated in the establishment of cell-cell contacts. Here, we show that Densin-180, which has been identified as a constituent of the postsynaptic density in excitatory synapses interacts with the postsynaptic scaffold protein shank (shank1-3). The interaction involves a two-point attachment of the C-terminal region of Densin-180 with the Src homology 3 domain and the N-terminal part of the proline-rich region of shank proteins. The N-terminal leucine-rich repeat region, which is not involved in binding shank, targets Densin-180 to the plasma membrane in transfected cells and to the basolateral membrane of epithelial cells. Nevertheless, coexpression of shank leads to a redirection of Densin-180 into intracellular clusters. In cultured hippocampal neurons, Densin-180 overexpression induces excessive branching of neuronal dendrites, which occurs at the expense of clusters for the postsynaptic marker PSD-95. Coexpression of shank3 abrogates branch formation and targets Densin-180 into postsynaptic clusters instead. Shank blocks binding of -catenin but not CaM kinase II to Densin-180; because -catenin has been shown to induce branching and neurite formation, our data suggest a mechanism where shank could block the activation of a Densin-180-dependent signaling pathway by -catenin.

Key words: leucine-rich repeats; ProSAP; PDZ domain; LAP proteins; proline-rich region; dendrite branching

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Received July 7, 2004; revised October 27, 2004; accepted November 17, 2004.

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