Loading…
Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes
Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine 36 → alanine (Ser 36 → Ala), serine 36 → glycine (ser 36 → Gly), and phenylalanine 37 → tryptophan (Phe...
Saved in:
| Published in: | Neuroscience letters 1996-11, Vol.219 (3), p.183-186 |
|---|---|
| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523 |
| container_end_page | 186 |
| container_issue | 3 |
| container_start_page | 183 |
| container_title | Neuroscience letters |
| container_volume | 219 |
| creator | Watson, J.B. Margulies, J.E. Coulter, P.M. Gerendasy, D.D. Sutcliffe, J.G. Cohen, R.W. |
| description | Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in
Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine
36 → alanine (Ser
36 → Ala), serine
36 → glycine (ser
36 → Gly), and phenylalanine
37 → tryptophan (Phe
37 → Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca
2+-dependent Cl
− currents in oocytes similar to control oocytes. A serine
36 → aspartate (Ser
36 → Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-triphosphate (IP3), diacylglycerol (DAG) and intracellular Ca
2+. |
| doi_str_mv | 10.1016/S0304-3940(96)13203-1 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_15844874</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0304394096132031</els_id><sourcerecordid>15844874</sourcerecordid><originalsourceid>FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523</originalsourceid><addsrcrecordid>eNqFkMFq3DAQhkVISbbbPkLAhxLagxvJsizrVMrStIVAoUmhNyFL40TBljYaOZC3rza77LUgJJj_mxnxEXLB6GdGWXd1Szlta65a-lF1nxhvKK_ZCVmxXja1VLI5Jasjck7eIj5SSgUT7Rk565VkPaMr8nS9BJt9DGaqMC_OA1ZxrNCH-wlq9BmqZ5O8CRkrH6r8AJU10xzdMvlQDz64QlYuzqakpfH3hl8FWFK8TyaUUjl_IcTtUsZG-5IB35E3o5kQ3h_eNflz_e1u86O--fX95-brTW15r3LNrGuFdAMfQYEcDRv7zgwjHYyhUljLhKWcDaKRTgEdrJPMOdc3RjEnlWj4mlzu525TfFoAs549WpgmEyAuqJno27aXbQHFHrQpIiYY9Tb52aQXzajeqdavqvXOo1adflVd7jW5OCxYhhncsevgtuQfDrnB4mwsQqzHI9YIKrtmt_7LHoMi49lD0mg9BAvOJ7BZu-j_85F_EGGc_w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15844874</pqid></control><display><type>article</type><title>Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes</title><source>ScienceDirect Freedom Collection 2022-2024</source><creator>Watson, J.B. ; Margulies, J.E. ; Coulter, P.M. ; Gerendasy, D.D. ; Sutcliffe, J.G. ; Cohen, R.W.</creator><creatorcontrib>Watson, J.B. ; Margulies, J.E. ; Coulter, P.M. ; Gerendasy, D.D. ; Sutcliffe, J.G. ; Cohen, R.W.</creatorcontrib><description>Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in
Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine
36 → alanine (Ser
36 → Ala), serine
36 → glycine (ser
36 → Gly), and phenylalanine
37 → tryptophan (Phe
37 → Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca
2+-dependent Cl
− currents in oocytes similar to control oocytes. A serine
36 → aspartate (Ser
36 → Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-triphosphate (IP3), diacylglycerol (DAG) and intracellular Ca
2+.</description><identifier>ISSN: 0304-3940</identifier><identifier>EISSN: 1872-7972</identifier><identifier>DOI: 10.1016/S0304-3940(96)13203-1</identifier><identifier>PMID: 8971810</identifier><identifier>CODEN: NELED5</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; Calmodulin - metabolism ; Calmodulin-binding mutants ; Calmodulin-Binding Proteins - genetics ; Calmodulin-Binding Proteins - metabolism ; Chlorides - physiology ; Dendritic protein ; Electric Conductivity ; Female ; Fundamental and applied biological sciences. Psychology ; Genetic Variation ; Long term potentiation-associated protein ; Molecular Sequence Data ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurogranin ; Oocytes - metabolism ; Patch-Clamp Techniques ; Protein kinase C substrate ; Proteins ; Serotonin - pharmacology ; Xenopus ; Xenopus laevis ; ‘IQ’ motif</subject><ispartof>Neuroscience letters, 1996-11, Vol.219 (3), p.183-186</ispartof><rights>1996</rights><rights>1997 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523</citedby><cites>FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2507624$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8971810$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Watson, J.B.</creatorcontrib><creatorcontrib>Margulies, J.E.</creatorcontrib><creatorcontrib>Coulter, P.M.</creatorcontrib><creatorcontrib>Gerendasy, D.D.</creatorcontrib><creatorcontrib>Sutcliffe, J.G.</creatorcontrib><creatorcontrib>Cohen, R.W.</creatorcontrib><title>Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes</title><title>Neuroscience letters</title><addtitle>Neurosci Lett</addtitle><description>Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in
Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine
36 → alanine (Ser
36 → Ala), serine
36 → glycine (ser
36 → Gly), and phenylalanine
37 → tryptophan (Phe
37 → Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca
2+-dependent Cl
− currents in oocytes similar to control oocytes. A serine
36 → aspartate (Ser
36 → Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-triphosphate (IP3), diacylglycerol (DAG) and intracellular Ca
2+.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Calmodulin - metabolism</subject><subject>Calmodulin-binding mutants</subject><subject>Calmodulin-Binding Proteins - genetics</subject><subject>Calmodulin-Binding Proteins - metabolism</subject><subject>Chlorides - physiology</subject><subject>Dendritic protein</subject><subject>Electric Conductivity</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Variation</subject><subject>Long term potentiation-associated protein</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurogranin</subject><subject>Oocytes - metabolism</subject><subject>Patch-Clamp Techniques</subject><subject>Protein kinase C substrate</subject><subject>Proteins</subject><subject>Serotonin - pharmacology</subject><subject>Xenopus</subject><subject>Xenopus laevis</subject><subject>‘IQ’ motif</subject><issn>0304-3940</issn><issn>1872-7972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkMFq3DAQhkVISbbbPkLAhxLagxvJsizrVMrStIVAoUmhNyFL40TBljYaOZC3rza77LUgJJj_mxnxEXLB6GdGWXd1Szlta65a-lF1nxhvKK_ZCVmxXja1VLI5Jasjck7eIj5SSgUT7Rk565VkPaMr8nS9BJt9DGaqMC_OA1ZxrNCH-wlq9BmqZ5O8CRkrH6r8AJU10xzdMvlQDz64QlYuzqakpfH3hl8FWFK8TyaUUjl_IcTtUsZG-5IB35E3o5kQ3h_eNflz_e1u86O--fX95-brTW15r3LNrGuFdAMfQYEcDRv7zgwjHYyhUljLhKWcDaKRTgEdrJPMOdc3RjEnlWj4mlzu525TfFoAs549WpgmEyAuqJno27aXbQHFHrQpIiYY9Tb52aQXzajeqdavqvXOo1adflVd7jW5OCxYhhncsevgtuQfDrnB4mwsQqzHI9YIKrtmt_7LHoMi49lD0mg9BAvOJ7BZu-j_85F_EGGc_w</recordid><startdate>19961129</startdate><enddate>19961129</enddate><creator>Watson, J.B.</creator><creator>Margulies, J.E.</creator><creator>Coulter, P.M.</creator><creator>Gerendasy, D.D.</creator><creator>Sutcliffe, J.G.</creator><creator>Cohen, R.W.</creator><general>Elsevier Ireland Ltd</general><general>Elsevier</general><scope>IQODW</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>7QP</scope><scope>7TK</scope></search><sort><creationdate>19961129</creationdate><title>Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes</title><author>Watson, J.B. ; Margulies, J.E. ; Coulter, P.M. ; Gerendasy, D.D. ; Sutcliffe, J.G. ; Cohen, R.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Calmodulin - metabolism</topic><topic>Calmodulin-binding mutants</topic><topic>Calmodulin-Binding Proteins - genetics</topic><topic>Calmodulin-Binding Proteins - metabolism</topic><topic>Chlorides - physiology</topic><topic>Dendritic protein</topic><topic>Electric Conductivity</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Variation</topic><topic>Long term potentiation-associated protein</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurogranin</topic><topic>Oocytes - metabolism</topic><topic>Patch-Clamp Techniques</topic><topic>Protein kinase C substrate</topic><topic>Proteins</topic><topic>Serotonin - pharmacology</topic><topic>Xenopus</topic><topic>Xenopus laevis</topic><topic>‘IQ’ motif</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watson, J.B.</creatorcontrib><creatorcontrib>Margulies, J.E.</creatorcontrib><creatorcontrib>Coulter, P.M.</creatorcontrib><creatorcontrib>Gerendasy, D.D.</creatorcontrib><creatorcontrib>Sutcliffe, J.G.</creatorcontrib><creatorcontrib>Cohen, R.W.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><jtitle>Neuroscience letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watson, J.B.</au><au>Margulies, J.E.</au><au>Coulter, P.M.</au><au>Gerendasy, D.D.</au><au>Sutcliffe, J.G.</au><au>Cohen, R.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes</atitle><jtitle>Neuroscience letters</jtitle><addtitle>Neurosci Lett</addtitle><date>1996-11-29</date><risdate>1996</risdate><volume>219</volume><issue>3</issue><spage>183</spage><epage>186</epage><pages>183-186</pages><issn>0304-3940</issn><eissn>1872-7972</eissn><coden>NELED5</coden><abstract>Single-site variants in the calmodulin-binding domain of RC3/neurogranin were heterologously expressed in
Xenopus oocytes to examine their effects on serotonin-evoked currents. RC3 variants serine
36 → alanine (Ser
36 → Ala), serine
36 → glycine (ser
36 → Gly), and phenylalanine
37 → tryptophan (Phe
37 → Trp), which bind calmodulin but are deficient in protein kinase C (PKC) phosphorylation, display serotonin-evoked Ca
2+-dependent Cl
− currents in oocytes similar to control oocytes. A serine
36 → aspartate (Ser
36 → Asp) variant, which does not bind calmodulin and mimics the PKC-phosphorylated state of RC3, significantly enhances serotonin-evoked currents in a manner similar to wild-type. The results suggest that RC3 not only regulates the availability of free calmodulin in a dendritic spine but also, when phosphorylated, independently stimulates G-protein coupled second messenger pathways that generate inositol 1,4,5-triphosphate (IP3), diacylglycerol (DAG) and intracellular Ca
2+.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>8971810</pmid><doi>10.1016/S0304-3940(96)13203-1</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0304-3940 |
| ispartof | Neuroscience letters, 1996-11, Vol.219 (3), p.183-186 |
| issn | 0304-3940 1872-7972 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15844874 |
| source | ScienceDirect Freedom Collection 2022-2024 |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences Calmodulin - metabolism Calmodulin-binding mutants Calmodulin-Binding Proteins - genetics Calmodulin-Binding Proteins - metabolism Chlorides - physiology Dendritic protein Electric Conductivity Female Fundamental and applied biological sciences. Psychology Genetic Variation Long term potentiation-associated protein Molecular Sequence Data Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurogranin Oocytes - metabolism Patch-Clamp Techniques Protein kinase C substrate Proteins Serotonin - pharmacology Xenopus Xenopus laevis ‘IQ’ motif |
| title | Functional studies of single-site variants in the calmodulin-binding domain of RC3/neurogranin in Xenopus oocytes |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T15%3A05%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20studies%20of%20single-site%20variants%20in%20the%20calmodulin-binding%20domain%20of%20RC3/neurogranin%20in%20Xenopus%20oocytes&rft.jtitle=Neuroscience%20letters&rft.au=Watson,%20J.B.&rft.date=1996-11-29&rft.volume=219&rft.issue=3&rft.spage=183&rft.epage=186&rft.pages=183-186&rft.issn=0304-3940&rft.eissn=1872-7972&rft.coden=NELED5&rft_id=info:doi/10.1016/S0304-3940(96)13203-1&rft_dat=%3Cproquest_cross%3E15844874%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c389t-1cd457db3fe9e7fa1f86abf0baa075cc15c031b527d9e0bcd71ddd82a91d79523%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=15844874&rft_id=info:pmid/8971810&rfr_iscdi=true |