Evidence That Calmodulin Binding to the Dopamine D2 Receptor Enhances Receptor Signaling
The Ca2+ sensor calmodulin (CaM) regulates numerous proteins involved in G protein-coupled receptor (GPCR) signaling. CaM binds directly to some GPCRs, including the dopamine D2 receptor. We confirmed that the third intracellular loop of the D2 receptor is a direct contact point for CaM binding usin...
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| Veröffentlicht in: | Journal of receptors and signal transduction 2007, Vol.27 (1), p.47-65 |
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| container_title | Journal of receptors and signal transduction |
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| creator | LIU, YONG BUCK, DAVID C. MACEY, TARA A. LAN, HONGXIANG NEVE, KIM A. |
| description | The Ca2+ sensor calmodulin (CaM) regulates numerous proteins involved in G protein-coupled receptor (GPCR) signaling. CaM binds directly to some GPCRs, including the dopamine D2 receptor. We confirmed that the third intracellular loop of the D2 receptor is a direct contact point for CaM binding using coimmunoprecipitation and a polyHis pull-down assay, and we determined that the D2-like receptor agonist 7-OH-DPAT increased the colocalization of the D2 receptor and endogenous CaM in both 293 cells and in primary neostriatal cultures. The N-terminal three or four residues of D2-IC3 were required for the binding of CaM; mutation of three of these residues in the full-length receptor (I210C/K211C/I212C) decreased the coprecipitation of the D2 receptor and CaM and also significantly decreased D2 receptor signaling, without altering the coupling of the receptor to G proteins. Taken together, these findings suggest that binding of CaM to the dopamine D2 receptor enhances D2 receptor signaling. |
| doi_str_mv | 10.1080/10799890601094152 |
| format | Article |
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CaM binds directly to some GPCRs, including the dopamine D2 receptor. We confirmed that the third intracellular loop of the D2 receptor is a direct contact point for CaM binding using coimmunoprecipitation and a polyHis pull-down assay, and we determined that the D2-like receptor agonist 7-OH-DPAT increased the colocalization of the D2 receptor and endogenous CaM in both 293 cells and in primary neostriatal cultures. The N-terminal three or four residues of D2-IC3 were required for the binding of CaM; mutation of three of these residues in the full-length receptor (I210C/K211C/I212C) decreased the coprecipitation of the D2 receptor and CaM and also significantly decreased D2 receptor signaling, without altering the coupling of the receptor to G proteins. Taken together, these findings suggest that binding of CaM to the dopamine D2 receptor enhances D2 receptor signaling.</description><identifier>ISSN: 1079-9893</identifier><identifier>EISSN: 1532-4281</identifier><identifier>DOI: 10.1080/10799890601094152</identifier><identifier>PMID: 17365509</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Adenylate cyclase ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Calmodulin ; Calmodulin - agonists ; Calmodulin - metabolism ; Calmodulin - pharmacology ; Cell Line ; Colforsin - pharmacology ; Cyclic AMP - metabolism ; D2 Receptor ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Humans ; Mitogen-activated protein kinase ; Molecular Sequence Data ; Neostriatum - cytology ; Neostriatum - metabolism ; Neurons - metabolism ; Protein:protein interaction ; Receptor signaling ; Receptors, Dopamine D2 - genetics ; Receptors, Dopamine D2 - metabolism ; Signal Transduction ; Transfection</subject><ispartof>Journal of receptors and signal transduction, 2007, Vol.27 (1), p.47-65</ispartof><rights>2007 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/10799890601094152$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/10799890601094152$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>314,780,784,4024,27923,27924,27925,59647,59753,60436,60542,61221,61256,61402,61437</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17365509$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LIU, YONG</creatorcontrib><creatorcontrib>BUCK, DAVID C.</creatorcontrib><creatorcontrib>MACEY, TARA A.</creatorcontrib><creatorcontrib>LAN, HONGXIANG</creatorcontrib><creatorcontrib>NEVE, KIM A.</creatorcontrib><title>Evidence That Calmodulin Binding to the Dopamine D2 Receptor Enhances Receptor Signaling</title><title>Journal of receptors and signal transduction</title><addtitle>J Recept Signal Transduct Res</addtitle><description>The Ca2+ sensor calmodulin (CaM) regulates numerous proteins involved in G protein-coupled receptor (GPCR) signaling. CaM binds directly to some GPCRs, including the dopamine D2 receptor. We confirmed that the third intracellular loop of the D2 receptor is a direct contact point for CaM binding using coimmunoprecipitation and a polyHis pull-down assay, and we determined that the D2-like receptor agonist 7-OH-DPAT increased the colocalization of the D2 receptor and endogenous CaM in both 293 cells and in primary neostriatal cultures. The N-terminal three or four residues of D2-IC3 were required for the binding of CaM; mutation of three of these residues in the full-length receptor (I210C/K211C/I212C) decreased the coprecipitation of the D2 receptor and CaM and also significantly decreased D2 receptor signaling, without altering the coupling of the receptor to G proteins. Taken together, these findings suggest that binding of CaM to the dopamine D2 receptor enhances D2 receptor signaling.</description><subject>Adenylate cyclase</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Calmodulin</subject><subject>Calmodulin - agonists</subject><subject>Calmodulin - metabolism</subject><subject>Calmodulin - pharmacology</subject><subject>Cell Line</subject><subject>Colforsin - pharmacology</subject><subject>Cyclic AMP - metabolism</subject><subject>D2 Receptor</subject><subject>Extracellular Signal-Regulated MAP Kinases - metabolism</subject><subject>Humans</subject><subject>Mitogen-activated protein kinase</subject><subject>Molecular Sequence Data</subject><subject>Neostriatum - cytology</subject><subject>Neostriatum - metabolism</subject><subject>Neurons - metabolism</subject><subject>Protein:protein interaction</subject><subject>Receptor signaling</subject><subject>Receptors, Dopamine D2 - genetics</subject><subject>Receptors, Dopamine D2 - metabolism</subject><subject>Signal Transduction</subject><subject>Transfection</subject><issn>1079-9893</issn><issn>1532-4281</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctKxTAQhoMo3h_AjXTlrjpJmyZBN3o8XkAQvIC7EJv0NNImx6RVztsbURERcTXDzPfN4h-EdjDsY-BwgIEJwQVUgEGUmJIltI5pQfKScLyc-rTPE1CsoY0YnwCwYBhW0RpmRUUpiHX0MH2x2rjaZHetGrKJ6nqvx8667MQ6bd0sG3w2tCY79XPVW5cakt2Y2swHH7Kpa1Vy4_fk1s6cSvpsC600qotm-7Nuovuz6d3kIr-6Pr-cHF_lllQw5I-YiKLGWhdGUAV1WVYNpzVhnCgQQDiUhFYlLzTlZSMEFVVdakVNYyqsBC420d7H3Xnwz6OJg-xtrE3XKWf8GCUDwghm8C9IQFSMs_eLu5_g-NgbLefB9ios5FdoCTj6AKxrfOjVqw-dloNadD40IQVioywwyPcfyV8_SvrhD701qhvaWgUjn_wYUnxR_m2_Afblkmo</recordid><startdate>2007</startdate><enddate>2007</enddate><creator>LIU, YONG</creator><creator>BUCK, DAVID C.</creator><creator>MACEY, TARA A.</creator><creator>LAN, HONGXIANG</creator><creator>NEVE, KIM A.</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QP</scope><scope>7X8</scope></search><sort><creationdate>2007</creationdate><title>Evidence That Calmodulin Binding to the Dopamine D2 Receptor Enhances Receptor Signaling</title><author>LIU, YONG ; BUCK, DAVID C. ; MACEY, TARA A. ; LAN, HONGXIANG ; NEVE, KIM A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i260t-b1293c1dd3e95a0c446f85c2782a0902804256483d584f99596c4da5efe61a913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenylate cyclase</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Calmodulin</topic><topic>Calmodulin - agonists</topic><topic>Calmodulin - metabolism</topic><topic>Calmodulin - pharmacology</topic><topic>Cell Line</topic><topic>Colforsin - pharmacology</topic><topic>Cyclic AMP - metabolism</topic><topic>D2 Receptor</topic><topic>Extracellular Signal-Regulated MAP Kinases - metabolism</topic><topic>Humans</topic><topic>Mitogen-activated protein kinase</topic><topic>Molecular Sequence Data</topic><topic>Neostriatum - cytology</topic><topic>Neostriatum - metabolism</topic><topic>Neurons - metabolism</topic><topic>Protein:protein interaction</topic><topic>Receptor signaling</topic><topic>Receptors, Dopamine D2 - genetics</topic><topic>Receptors, Dopamine D2 - metabolism</topic><topic>Signal Transduction</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LIU, YONG</creatorcontrib><creatorcontrib>BUCK, DAVID C.</creatorcontrib><creatorcontrib>MACEY, TARA A.</creatorcontrib><creatorcontrib>LAN, HONGXIANG</creatorcontrib><creatorcontrib>NEVE, KIM A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of receptors and signal transduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LIU, YONG</au><au>BUCK, DAVID C.</au><au>MACEY, TARA A.</au><au>LAN, HONGXIANG</au><au>NEVE, KIM A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence That Calmodulin Binding to the Dopamine D2 Receptor Enhances Receptor Signaling</atitle><jtitle>Journal of receptors and signal transduction</jtitle><addtitle>J Recept Signal Transduct Res</addtitle><date>2007</date><risdate>2007</risdate><volume>27</volume><issue>1</issue><spage>47</spage><epage>65</epage><pages>47-65</pages><issn>1079-9893</issn><eissn>1532-4281</eissn><abstract>The Ca2+ sensor calmodulin (CaM) regulates numerous proteins involved in G protein-coupled receptor (GPCR) signaling. CaM binds directly to some GPCRs, including the dopamine D2 receptor. We confirmed that the third intracellular loop of the D2 receptor is a direct contact point for CaM binding using coimmunoprecipitation and a polyHis pull-down assay, and we determined that the D2-like receptor agonist 7-OH-DPAT increased the colocalization of the D2 receptor and endogenous CaM in both 293 cells and in primary neostriatal cultures. The N-terminal three or four residues of D2-IC3 were required for the binding of CaM; mutation of three of these residues in the full-length receptor (I210C/K211C/I212C) decreased the coprecipitation of the D2 receptor and CaM and also significantly decreased D2 receptor signaling, without altering the coupling of the receptor to G proteins. Taken together, these findings suggest that binding of CaM to the dopamine D2 receptor enhances D2 receptor signaling.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>17365509</pmid><doi>10.1080/10799890601094152</doi><tpages>19</tpages></addata></record> |
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| ispartof | Journal of receptors and signal transduction, 2007, Vol.27 (1), p.47-65 |
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| source | MEDLINE; Taylor & Francis Medical Library - CRKN; Taylor & Francis Journals Complete |
| subjects | Adenylate cyclase Amino Acid Motifs Amino Acid Sequence Binding Sites Calmodulin Calmodulin - agonists Calmodulin - metabolism Calmodulin - pharmacology Cell Line Colforsin - pharmacology Cyclic AMP - metabolism D2 Receptor Extracellular Signal-Regulated MAP Kinases - metabolism Humans Mitogen-activated protein kinase Molecular Sequence Data Neostriatum - cytology Neostriatum - metabolism Neurons - metabolism Protein:protein interaction Receptor signaling Receptors, Dopamine D2 - genetics Receptors, Dopamine D2 - metabolism Signal Transduction Transfection |
| title | Evidence That Calmodulin Binding to the Dopamine D2 Receptor Enhances Receptor Signaling |
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