GODZ-Mediated Palmitoylation of GABAAReceptors Is Required for Normal Assembly and Function of GABAergic Inhibitory Synapses

• DOI: 10.1523/jneurosci.4214-06.2006
• Publication Date: 2006-12-06T19:08:49Z
• Authors: Cheng Fang; Lunbin Deng; Cheryl A. Keller; Masaki Fukata; Yuko Fukata; Gong Chen; Bernhard Lüscher
• Keywords: Palmitoylation; HEK 293 cells; Gephyrin; Colocalization; Synaptogenesis

Golgi-specific DHHC (Asp-His-His-Cys) zinc finger protein (GODZ) is a family palmitoyl acyltransferase that implicated in palmitoylation and regulated trafficking of diverse substrates function either at inhibitory or excitatory synapses. Of particular interest the γ2 subunit GABA A receptors, which required for targeting these receptors to Here, we report GODZ and, lesser extent, its close paralog sertoli cell gene with domain-β (SERZ-β) are main members enzymes able palmitoylate heterologous cells. Yeast two-hybrid colocalization assays human embryonic kidney 293T (HEK293T) cells indicate SERZ-β show indistinguishable palmitoylation-dependent interaction subunit. After coexpression HEK293T cells, they form homomultimers heteromultimers, as shown by coimmunoprecipitation vivo cross-linking experiments. Analyses neurons transfected dominant-negative (GODZ C157S ) plasmid-based GODZ-specific RNAi normal accumulation synapses, whole-cell synaptic GABAergic indirectly, innervation. Unexpectedly, was found be dispensable postsynaptic AMPA receptor-mediated glutamatergic transmission. We conclude GODZ-mediated possibly other contributes selectively formation