SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor
Autor: | Joohong Ahnn, Jungsoo Lee, Eunhye Park, Chang Hoon Jee, Jae Ran Yu, Jin I. Lee, Eunjoon Kim, Byung Jae Park, Won Hae Lee |
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Rok vydání: | 2003 |
Předmět: |
Scaffold protein
Periodicity PDZ domain Molecular Sequence Data Biophysics Receptors Cytoplasmic and Nuclear Sequence Homology Nerve Tissue Proteins Inositol-1 4 5-trisphosphate receptor Biochemistry Receptor localization Structural Biology Genetics Animals Inositol 1 4 5-Trisphosphate Receptors 5-HT5A receptor Tissue Distribution Amino Acid Sequence RNA Small Interfering Receptor Caenorhabditis elegans Caenorhabditis elegans Proteins Defecation Molecular Biology Defecation cycle Adaptor Proteins Signal Transducing Scaffolding protein biology Signal transducing adaptor protein Postsynaptic density Cell Biology biology.organism_classification Cell biology Mutation Defecation rhythm Calcium Channels Carrier Proteins |
Zdroj: | FEBS letters. 561(1-3) |
ISSN: | 0014-5793 |
Popis: | 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 (IP3) receptor, resulted in animals with altered defecation rhythm. Our data suggest a possible role of SHN-1 in affecting function of IP3 receptors in C. elegans. |
Databáze: | OpenAIRE |
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