Analyses of Localization and Function of C. elegans Synaptic Proteins

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In order to obtain genetic tools to study further the formation of pre- and postsynaptic structures during development as well as the mechanisms of targeting postsynaptic proteins to synapses, we searched C. elegans genome for genes homologous to postsynaptic proteins recently identified in mammalian postsynaptic structures. We confirmed their expression by amplifying cDNA fragments. Sequencing of these cDNA fragments revealed genomic organization and amino acid sequence of the protein. Some of these proteins possess highly conserved amino acid sequences and overall domain organization, A C. elegans homologue (C25F6.2) of Drosophila Discs Large and mammalian PSD-95/SAP90 family proteins consists of three PDZ domains, one SH3 domain and a guanylate kinase domain. A homologue (formerly A assigned as K01A6.2 and K01A6.1) of S-SCAM/ARIP/MAGI family proteins associating with various kinds of receptor proteins consists of one guanylate kinase domain, two tandem WW domains and five PDZ domains. A homologue (C33B4.3) of synamon/shank, proteins coupling NMDAR/PSD-95 complex and mGluR/Homer complex, possesses ankyrin repeats, a PDZ domain and a SAM domain. Characterization of these C. elegans genes suggests importance of molecular structures that may be involved the postsynaptic specialization.