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SHN‐1, a Shank homologue in C. elegans , affects defecation rhythm via the inositol‐1,4,5‐trisphosphate receptor
Author(s) -
Jee Changhoon,
Lee Jungsoo,
Lee Jin Il,
Lee Won Hae,
Park Byung-Jae,
Yu Jae-Ran,
Park Eunhye,
Kim Eunjoon,
Ahnn Joohong
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00107-3
Subject(s) - inositol , rhythm , receptor , chemistry , endocrinology , microbiology and biotechnology , medicine , biology , neuroscience , biochemistry
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 .