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3120 The Journal of Neuroscience, March 21, 2007 27(12):3120 3130 Cellular/Molecular Fragile X Mental Retardation Protein Induces Synapse Loss through Acute Postsynaptic Translational Regulation Brad

Because the basal ganglia are critically involved in various neurocognitive functions, these findings have important implications in the pathogenesis of these neurological disorders. Using a recombinant fragment of fragile X (frag) gene and a transgenic mouse model of autism and mental retardation, we found that frag protein mediates synapse loss via protein kinase C alpha-dependent, synaptic plasticity-driven gene regulation by interacting with CTC. Furthermore, we identified a CTC binding motif on frag protein that is required for robust induction of neural synapse loss. We demonstrate that frag protein regulates neural synapse loss and synaptic plasticity, which together result in abnormal synaptic dynamics and impaired function. The findings have broad implications for the understanding of fragile X syndrome and autism. Biological psychiatry, 2009, 53(7):865 – 890 Sci., 2014, 7(6), pp. The frag protein family, consisting of the proteins Floridian (FN), frag-1, and frag-2, has recently revealed itself as being important for a broad spectrum of functions related to synaptic organization (J.C. Gaff our, K.C. Socks, J.M. Furlong, D. Key, J.E. Meany, D.K. CSU, and K.J. Shackelford, unpublished observations). Here we reveal additional functions for these related, but non-synaptic, proteins, which include regulation of cell adhesion, cell growth, cell motility, and cell apoptosis. Frag-1 and frag-2 belong to the frag protein family as do a number of genes in different subfamilies, including the fibrillin-like synaptic II family. Interestingly, all the described functions of frag proteins are controlled by a family of intracellular proteins that are known to be related to postsynaptic density. This family of proteins, known as the synaptic proteins (SNP), regulates the formation of dendritic spines through a series of intracellular processes that involve cell surface binding of a synaptic. Using a synapsin-based covalent immunoglobulin binding protocol, we show that both frags-1 and -2 bind to SNP while frags-3 and -6 bind to ASPCA.

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