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- W2049205004 abstract "Protein localization in the postsynaptic density (PSD) of neurons is mediated by scaffolding proteins such as PSD-95 and Shank, which ensure proper function of receptors at the membrane. The Shank family of scaffolding proteins contain PDZ (PSD-95, Dlg, and ZO-1) domains and have been implicated in the localizations of many receptor proteins including glutamate receptors in mammals. We have identified and characterized shn-1, the only homologue of Shank in Caenorhabditis elegans. The shn-1 gene shows approximately 40% identity over 1000 amino acids to rat Shanks. SHN-1 protein is localized in various tissues including neurons, pharynx and intestine. RNAi suppression of SHN-1 did not cause lethality or developmental abnormality. However, suppression of SHN-1 in the itr-1 (sa73) mutant, which has a defective inositol-1,4,5-trisphosphate (IP(3)) receptor, resulted in animals with altered defecation rhythm. Our data suggest a possible role of SHN-1 in affecting function of IP(3) receptors in C. elegans." @default.
- W2049205004 created "2016-06-24" @default.
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- W2049205004 date "2004-02-13" @default.
- W2049205004 modified "2023-10-14" @default.
- W2049205004 title "SHN-1, a Shank homologue in<i>C. elegans</i>, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor" @default.
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- W2049205004 doi "https://doi.org/10.1016/s0014-5793(04)00107-3" @default.
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