SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor
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...
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| Veröffentlicht in: | FEBS letters 2004-03, Vol.561 (1), p.29-36 |
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| creator | Jee, Changhoon Lee, Jungsoo Lee, Jin Il Lee, Won Hae Park, Byung-Jae Yu, Jae-Ran Park, Eunhye Kim, Eunjoon Ahnn, Joohong |
| description | 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. |
| doi_str_mv | 10.1016/S0014-5793(04)00107-3 |
| format | Article |
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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.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(04)00107-3</identifier><identifier>PMID: 15013747</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans - physiology ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - physiology ; Calcium Channels - genetics ; Carrier Proteins - genetics ; Carrier Proteins - physiology ; Defecation - genetics ; Defecation cycle ; Inositol 1,4,5-Trisphosphate Receptors ; Inositol-1,4,5-trisphosphate receptor ; Molecular Sequence Data ; Mutation ; Nerve Tissue Proteins ; Periodicity ; Postsynaptic density ; Receptor localization ; Receptors, Cytoplasmic and Nuclear - genetics ; RNA, Small Interfering - pharmacology ; Scaffolding protein ; Sequence Homology ; Tissue Distribution</subject><ispartof>FEBS letters, 2004-03, Vol.561 (1), p.29-36</ispartof><rights>2004 Federation of European Biochemical Societies</rights><rights>FEBS Letters 561 (2004) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4733-f65b91bab02bb3000c242254de7249ce14a407d61558c79bd9f0727073fc5b9e3</citedby><cites>FETCH-LOGICAL-c4733-f65b91bab02bb3000c242254de7249ce14a407d61558c79bd9f0727073fc5b9e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2804%2900107-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579304001073$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3536,27903,27904,45553,45554,46387,46811,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15013747$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jee, Changhoon</creatorcontrib><creatorcontrib>Lee, Jungsoo</creatorcontrib><creatorcontrib>Lee, Jin Il</creatorcontrib><creatorcontrib>Lee, Won Hae</creatorcontrib><creatorcontrib>Park, Byung-Jae</creatorcontrib><creatorcontrib>Yu, Jae-Ran</creatorcontrib><creatorcontrib>Park, Eunhye</creatorcontrib><creatorcontrib>Kim, Eunjoon</creatorcontrib><creatorcontrib>Ahnn, Joohong</creatorcontrib><title>SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>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.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caenorhabditis elegans - physiology</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - physiology</subject><subject>Calcium Channels - genetics</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - physiology</subject><subject>Defecation - genetics</subject><subject>Defecation cycle</subject><subject>Inositol 1,4,5-Trisphosphate Receptors</subject><subject>Inositol-1,4,5-trisphosphate receptor</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nerve Tissue Proteins</subject><subject>Periodicity</subject><subject>Postsynaptic density</subject><subject>Receptor localization</subject><subject>Receptors, Cytoplasmic and Nuclear - genetics</subject><subject>RNA, Small Interfering - pharmacology</subject><subject>Scaffolding protein</subject><subject>Sequence Homology</subject><subject>Tissue Distribution</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE9PGzEQxS1UVFLoR6DyqSoSC_4bZ0-IRtBUQnBIe7a83lnWZXcdbAeUb19vEpUjPVij8bz3ZvRD6JSSC0ro9HJJCBWFVCX_RsRZbogq-AGa0JniBRfT2Qc0-Sc5Qp9i_ENyP6PlR3REJaFcCTVBfrm4L-g5NnjZmuEJt773nX9cA3YDnl9g6ODRDDELmgZsiriGXE1yfsCh3aS2xy_O4NSOBh9d8l2OE-eySMHFVevzMwlwAAur5MMJOmxMF-Hzvh6j37c3v-aL4u7hx8_59V1hheK8aKayKmllKsKqiufDLROMSVGDYqK0QIURRNVTKuXMqrKqy4Yopojijc1O4Mfo6y53FfzzGmLSvYsWus4M4NdRK6oYl0xkodwJbfAxBmj0KrjehI2mRI-k9Za0HjFqIvSWtObZ92W_YF31UL-59mizYLETvLoONv-Xqm9vvrPtZBwQsf0ed13toiATe3EQdLQOBgu1y1yTrr1759q_jfefsQ</recordid><startdate>20040312</startdate><enddate>20040312</enddate><creator>Jee, Changhoon</creator><creator>Lee, Jungsoo</creator><creator>Lee, Jin Il</creator><creator>Lee, Won Hae</creator><creator>Park, Byung-Jae</creator><creator>Yu, Jae-Ran</creator><creator>Park, Eunhye</creator><creator>Kim, Eunjoon</creator><creator>Ahnn, Joohong</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040312</creationdate><title>SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor</title><author>Jee, Changhoon ; Lee, Jungsoo ; Lee, Jin Il ; Lee, Won Hae ; Park, Byung-Jae ; Yu, Jae-Ran ; Park, Eunhye ; Kim, Eunjoon ; Ahnn, Joohong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4733-f65b91bab02bb3000c242254de7249ce14a407d61558c79bd9f0727073fc5b9e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caenorhabditis elegans - physiology</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - physiology</topic><topic>Calcium Channels - genetics</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - physiology</topic><topic>Defecation - genetics</topic><topic>Defecation cycle</topic><topic>Inositol 1,4,5-Trisphosphate Receptors</topic><topic>Inositol-1,4,5-trisphosphate receptor</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Nerve Tissue Proteins</topic><topic>Periodicity</topic><topic>Postsynaptic density</topic><topic>Receptor localization</topic><topic>Receptors, Cytoplasmic and Nuclear - genetics</topic><topic>RNA, Small Interfering - pharmacology</topic><topic>Scaffolding protein</topic><topic>Sequence Homology</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jee, Changhoon</creatorcontrib><creatorcontrib>Lee, Jungsoo</creatorcontrib><creatorcontrib>Lee, Jin Il</creatorcontrib><creatorcontrib>Lee, Won Hae</creatorcontrib><creatorcontrib>Park, Byung-Jae</creatorcontrib><creatorcontrib>Yu, Jae-Ran</creatorcontrib><creatorcontrib>Park, Eunhye</creatorcontrib><creatorcontrib>Kim, Eunjoon</creatorcontrib><creatorcontrib>Ahnn, Joohong</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jee, Changhoon</au><au>Lee, Jungsoo</au><au>Lee, Jin Il</au><au>Lee, Won Hae</au><au>Park, Byung-Jae</au><au>Yu, Jae-Ran</au><au>Park, Eunhye</au><au>Kim, Eunjoon</au><au>Ahnn, Joohong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-03-12</date><risdate>2004</risdate><volume>561</volume><issue>1</issue><spage>29</spage><epage>36</epage><pages>29-36</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15013747</pmid><doi>10.1016/S0014-5793(04)00107-3</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2004-03, Vol.561 (1), p.29-36 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71723524 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Caenorhabditis elegans - physiology Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - physiology Calcium Channels - genetics Carrier Proteins - genetics Carrier Proteins - physiology Defecation - genetics Defecation cycle Inositol 1,4,5-Trisphosphate Receptors Inositol-1,4,5-trisphosphate receptor Molecular Sequence Data Mutation Nerve Tissue Proteins Periodicity Postsynaptic density Receptor localization Receptors, Cytoplasmic and Nuclear - genetics RNA, Small Interfering - pharmacology Scaffolding protein Sequence Homology Tissue Distribution |
| title | SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the inositol-1,4,5-trisphosphate receptor |
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