Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a new internal PDZ-recognition motif |
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Authors: | Lemaire Jean-François McPherson Peter S |
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Institution: | Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University Street, Montreal, Que., Canada H3A 2B4. |
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Abstract: | PDZ domains mediate protein interactions primarily through either classical recognition of carboxyl-terminal motifs or PDZ/PDZ domain associations. Several studies have also described internal modes of PDZ recognition, most of which depend on β-finger structures. Here, we describe a novel interaction between the PDZ domain of nNOS and Vac14, the activator of the PtdIns(3)P 5-kinase PIKfyve. Binding assays using various Vac14 deletion constructs revealed a β-finger independent interaction that is based on a novel internal motif. Mutational analyses reveal essential residues within the motif allowing us to define a new type of PDZ domain interaction. |
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Keywords: | Peptide motif PDZ nNOS Vac14 PIKfyve 5-HT2B receptor |
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