Functional importance of polymerization and localization of calsequestrin in C. elegans
Dual roles of calsequestrin (CSQ-1) being the Ca²⁺ donor and Ca²⁺ acceptor make it an excellent Ca²⁺-buffering protein within the sarcoplasmic reticulum (SR). We have isolated and characterized a calsequestrin (csq-1)-null mutant in Caenorhabditis elegans. To our surprise, this mutant csq-1(jh109) s...
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| Veröffentlicht in: | Journal of cell science 2007-05, Vol.120 (9), p.1551-1558 |
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| creator | Cho, J.H Ko, K.M Singaruvelu, Gunasekaran Lee, Wonhae Kang, Gil Bu Rho, Seong-Hwan Park, Byung-Jae Yu, Jae-Ran Kagawa, Hiroaki Eom, S.H Kim, D.H Ahnn, Joohong |
| description | Dual roles of calsequestrin (CSQ-1) being the Ca²⁺ donor and Ca²⁺ acceptor make it an excellent Ca²⁺-buffering protein within the sarcoplasmic reticulum (SR). We have isolated and characterized a calsequestrin (csq-1)-null mutant in Caenorhabditis elegans. To our surprise, this mutant csq-1(jh109) showed no gross defects in muscle development or function but, however, is highly sensitive to perturbation of Ca²⁺ homeostasis. By taking advantage of the viable null mutant, we investigated the domains of CSQ-1 that are important for polymerization and cellular localization, and required for its correct buffering functions. In transgenic animals rescued with various CSQ-1 constructs, the in vivo patterns of polymerization and localization of several mutated calsequestrins were observed to correlate with the structure-function relationship. Our results suggest that polymerization of CSQ-1 is essential but not sufficient for correct cellular localization and function of CSQ-1. In addition, direct interaction between CSQ-1 and the ryanodine receptor (RyR) was found for the first time, suggesting that the cellular localization of CSQ-1 in C. elegans is indeed modulated by RyR through a physical interaction. |
| doi_str_mv | 10.1242/jcs.001016 |
| format | Article |
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We have isolated and characterized a calsequestrin (csq-1)-null mutant in Caenorhabditis elegans. To our surprise, this mutant csq-1(jh109) showed no gross defects in muscle development or function but, however, is highly sensitive to perturbation of Ca²⁺ homeostasis. By taking advantage of the viable null mutant, we investigated the domains of CSQ-1 that are important for polymerization and cellular localization, and required for its correct buffering functions. In transgenic animals rescued with various CSQ-1 constructs, the in vivo patterns of polymerization and localization of several mutated calsequestrins were observed to correlate with the structure-function relationship. Our results suggest that polymerization of CSQ-1 is essential but not sufficient for correct cellular localization and function of CSQ-1. In addition, direct interaction between CSQ-1 and the ryanodine receptor (RyR) was found for the first time, suggesting that the cellular localization of CSQ-1 in C. elegans is indeed modulated by RyR through a physical interaction.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.001016</identifier><identifier>PMID: 17405817</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Caenorhabditis elegans Proteins - physiology ; Calcium - pharmacology ; Calsequestrin - genetics ; Calsequestrin - metabolism ; Calsequestrin - physiology ; Egtazic Acid - pharmacology ; Gene Deletion ; Locomotion - genetics ; Locomotion - physiology ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Muscles - metabolism ; Muscles - physiology ; Mutation ; Phenotype ; Polymers - chemistry ; Polymers - metabolism ; Protein Binding ; Protein Structure, Quaternary ; Reproduction - genetics ; Reproduction - physiology ; Ryanodine Receptor Calcium Release Channel - chemistry ; Ryanodine Receptor Calcium Release Channel - metabolism ; Sequence Homology, Amino Acid ; Structure-Activity Relationship ; Transfection</subject><ispartof>Journal of cell science, 2007-05, Vol.120 (9), p.1551-1558</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-221b1f746ed3d0b77dce251b3c8c9c7d95828569cfef4fb72b85532fed3b2d823</citedby><cites>FETCH-LOGICAL-c412t-221b1f746ed3d0b77dce251b3c8c9c7d95828569cfef4fb72b85532fed3b2d823</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3676,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17405817$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cho, J.H</creatorcontrib><creatorcontrib>Ko, K.M</creatorcontrib><creatorcontrib>Singaruvelu, Gunasekaran</creatorcontrib><creatorcontrib>Lee, Wonhae</creatorcontrib><creatorcontrib>Kang, Gil Bu</creatorcontrib><creatorcontrib>Rho, Seong-Hwan</creatorcontrib><creatorcontrib>Park, Byung-Jae</creatorcontrib><creatorcontrib>Yu, Jae-Ran</creatorcontrib><creatorcontrib>Kagawa, Hiroaki</creatorcontrib><creatorcontrib>Eom, S.H</creatorcontrib><creatorcontrib>Kim, D.H</creatorcontrib><creatorcontrib>Ahnn, Joohong</creatorcontrib><title>Functional importance of polymerization and localization of calsequestrin in C. elegans</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>Dual roles of calsequestrin (CSQ-1) being the Ca²⁺ donor and Ca²⁺ acceptor make it an excellent Ca²⁺-buffering protein within the sarcoplasmic reticulum (SR). We have isolated and characterized a calsequestrin (csq-1)-null mutant in Caenorhabditis elegans. To our surprise, this mutant csq-1(jh109) showed no gross defects in muscle development or function but, however, is highly sensitive to perturbation of Ca²⁺ homeostasis. By taking advantage of the viable null mutant, we investigated the domains of CSQ-1 that are important for polymerization and cellular localization, and required for its correct buffering functions. In transgenic animals rescued with various CSQ-1 constructs, the in vivo patterns of polymerization and localization of several mutated calsequestrins were observed to correlate with the structure-function relationship. Our results suggest that polymerization of CSQ-1 is essential but not sufficient for correct cellular localization and function of CSQ-1. In addition, direct interaction between CSQ-1 and the ryanodine receptor (RyR) was found for the first time, suggesting that the cellular localization of CSQ-1 in C. elegans is indeed modulated by RyR through a physical interaction.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Caenorhabditis elegans Proteins - physiology</subject><subject>Calcium - pharmacology</subject><subject>Calsequestrin - genetics</subject><subject>Calsequestrin - metabolism</subject><subject>Calsequestrin - physiology</subject><subject>Egtazic Acid - pharmacology</subject><subject>Gene Deletion</subject><subject>Locomotion - genetics</subject><subject>Locomotion - physiology</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Muscles - metabolism</subject><subject>Muscles - physiology</subject><subject>Mutation</subject><subject>Phenotype</subject><subject>Polymers - chemistry</subject><subject>Polymers - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Reproduction - genetics</subject><subject>Reproduction - physiology</subject><subject>Ryanodine Receptor Calcium Release Channel - chemistry</subject><subject>Ryanodine Receptor Calcium Release Channel - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-Activity Relationship</subject><subject>Transfection</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9LwzAUB_Agis7pxT9Ae_IgdOblR9MeZTgVBh50eAxpmoyOtqlJd5h_vZmdeBQCj-R9eITvQ-gK8AwII_cbHWYYA4bsCE2ACZEWQMUxmmBMIC04pWfoPIQNxliQQpyiMxAM8xzEBH0stp0eatepJqnb3vlBddokzia9a3at8fWX2rcT1VVJ47Rqfh8iibdgPrcmDL7uknjms8Q0Zq26cIFO7L57eahTtFo8vs-f0-Xr08v8YZlqBmRICYESrGCZqWiFSyEqbQiHkupcF1pUBc9JzrNCW2OZLQUpc84psZGXpMoJnaLbcW7v3c9PZFsHbZpGdcZtgxSYAc2E-BcSTHLGoYjwboTauxC8sbL3dav8TgKW-7xlzFuOeUd8fZi6LVtT_dFDwBHcjMAqJ9Xa10Gu3ggGGnchcEE5_QamDIVK</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Cho, J.H</creator><creator>Ko, K.M</creator><creator>Singaruvelu, Gunasekaran</creator><creator>Lee, Wonhae</creator><creator>Kang, Gil Bu</creator><creator>Rho, Seong-Hwan</creator><creator>Park, Byung-Jae</creator><creator>Yu, Jae-Ran</creator><creator>Kagawa, Hiroaki</creator><creator>Eom, S.H</creator><creator>Kim, D.H</creator><creator>Ahnn, Joohong</creator><general>The Company of Biologists Limited</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>20070501</creationdate><title>Functional importance of polymerization and localization of calsequestrin in C. elegans</title><author>Cho, J.H ; Ko, K.M ; Singaruvelu, Gunasekaran ; Lee, Wonhae ; Kang, Gil Bu ; Rho, Seong-Hwan ; Park, Byung-Jae ; Yu, Jae-Ran ; Kagawa, Hiroaki ; Eom, S.H ; Kim, D.H ; Ahnn, Joohong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-221b1f746ed3d0b77dce251b3c8c9c7d95828569cfef4fb72b85532fed3b2d823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Caenorhabditis elegans Proteins - physiology</topic><topic>Calcium - pharmacology</topic><topic>Calsequestrin - genetics</topic><topic>Calsequestrin - metabolism</topic><topic>Calsequestrin - physiology</topic><topic>Egtazic Acid - pharmacology</topic><topic>Gene Deletion</topic><topic>Locomotion - genetics</topic><topic>Locomotion - physiology</topic><topic>Models, Biological</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Muscles - metabolism</topic><topic>Muscles - physiology</topic><topic>Mutation</topic><topic>Phenotype</topic><topic>Polymers - chemistry</topic><topic>Polymers - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Reproduction - genetics</topic><topic>Reproduction - physiology</topic><topic>Ryanodine Receptor Calcium Release Channel - chemistry</topic><topic>Ryanodine Receptor Calcium Release Channel - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structure-Activity Relationship</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cho, J.H</creatorcontrib><creatorcontrib>Ko, K.M</creatorcontrib><creatorcontrib>Singaruvelu, Gunasekaran</creatorcontrib><creatorcontrib>Lee, Wonhae</creatorcontrib><creatorcontrib>Kang, Gil Bu</creatorcontrib><creatorcontrib>Rho, Seong-Hwan</creatorcontrib><creatorcontrib>Park, Byung-Jae</creatorcontrib><creatorcontrib>Yu, Jae-Ran</creatorcontrib><creatorcontrib>Kagawa, Hiroaki</creatorcontrib><creatorcontrib>Eom, S.H</creatorcontrib><creatorcontrib>Kim, D.H</creatorcontrib><creatorcontrib>Ahnn, Joohong</creatorcontrib><collection>AGRIS</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>MEDLINE - Academic</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cho, J.H</au><au>Ko, K.M</au><au>Singaruvelu, Gunasekaran</au><au>Lee, Wonhae</au><au>Kang, Gil Bu</au><au>Rho, Seong-Hwan</au><au>Park, Byung-Jae</au><au>Yu, Jae-Ran</au><au>Kagawa, Hiroaki</au><au>Eom, S.H</au><au>Kim, D.H</au><au>Ahnn, Joohong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional importance of polymerization and localization of calsequestrin in C. elegans</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>120</volume><issue>9</issue><spage>1551</spage><epage>1558</epage><pages>1551-1558</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Dual roles of calsequestrin (CSQ-1) being the Ca²⁺ donor and Ca²⁺ acceptor make it an excellent Ca²⁺-buffering protein within the sarcoplasmic reticulum (SR). We have isolated and characterized a calsequestrin (csq-1)-null mutant in Caenorhabditis elegans. To our surprise, this mutant csq-1(jh109) showed no gross defects in muscle development or function but, however, is highly sensitive to perturbation of Ca²⁺ homeostasis. By taking advantage of the viable null mutant, we investigated the domains of CSQ-1 that are important for polymerization and cellular localization, and required for its correct buffering functions. In transgenic animals rescued with various CSQ-1 constructs, the in vivo patterns of polymerization and localization of several mutated calsequestrins were observed to correlate with the structure-function relationship. Our results suggest that polymerization of CSQ-1 is essential but not sufficient for correct cellular localization and function of CSQ-1. In addition, direct interaction between CSQ-1 and the ryanodine receptor (RyR) was found for the first time, suggesting that the cellular localization of CSQ-1 in C. elegans is indeed modulated by RyR through a physical interaction.</abstract><cop>England</cop><pub>The Company of Biologists Limited</pub><pmid>17405817</pmid><doi>10.1242/jcs.001016</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of cell science, 2007-05, Vol.120 (9), p.1551-1558 |
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| subjects | Amino Acid Sequence Animals Binding Sites Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Caenorhabditis elegans Proteins - physiology Calcium - pharmacology Calsequestrin - genetics Calsequestrin - metabolism Calsequestrin - physiology Egtazic Acid - pharmacology Gene Deletion Locomotion - genetics Locomotion - physiology Models, Biological Models, Molecular Molecular Sequence Data Muscles - metabolism Muscles - physiology Mutation Phenotype Polymers - chemistry Polymers - metabolism Protein Binding Protein Structure, Quaternary Reproduction - genetics Reproduction - physiology Ryanodine Receptor Calcium Release Channel - chemistry Ryanodine Receptor Calcium Release Channel - metabolism Sequence Homology, Amino Acid Structure-Activity Relationship Transfection |
| title | Functional importance of polymerization and localization of calsequestrin in C. elegans |
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