Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel
The skeletal muscle Ca2+ release channel (RYR1) is regulated by calmodulin in both its Ca2+-free (apocalmodulin) and Ca2+-bound (Ca2+ calmodulin) states. Apocalmodulin is an activator of the channel, and Ca2+ calmodulin is an inhibitor of the channel. Both apocalmodulin and Ca2+ calmodulin binding s...
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| Veröffentlicht in: | Biochemistry (Easton) 1999-06, Vol.38 (26), p.8532-8537 |
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| creator | Moore, Catherine Porter Rodney, George Zhang, Jia-Zheng Santacruz-Toloza, Lucia Strasburg, Gale Hamilton, Susan L |
| description | The skeletal muscle Ca2+ release channel (RYR1) is regulated by calmodulin in both its Ca2+-free (apocalmodulin) and Ca2+-bound (Ca2+ calmodulin) states. Apocalmodulin is an activator of the channel, and Ca2+ calmodulin is an inhibitor of the channel. Both apocalmodulin and Ca2+ calmodulin binding sites on RYR1 are destroyed by a mild tryptic digestion of the sarcoplasmic reticulum membranes, but calmodulin (either form), bound to RYR1 prior to tryptic digestion, protects both the apocalmodulin and Ca2+ calmodulin sites from tryptic destruction. The protected sites are after arginines 3630 and 3637 on RYR1. These studies suggest that both Ca2+ calmodulin and apocalmodulin bind to the same or overlapping regions on RYR1 and block access of trypsin to sites at amino acids 3630 and 3637. This sequence is part of a predicted Ca2+ CaM binding site of amino acids 3614−3642 [Takeshima, H., et al. (1989) Nature 339, 439−445]. |
| doi_str_mv | 10.1021/bi9907431 |
| format | Article |
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Apocalmodulin is an activator of the channel, and Ca2+ calmodulin is an inhibitor of the channel. Both apocalmodulin and Ca2+ calmodulin binding sites on RYR1 are destroyed by a mild tryptic digestion of the sarcoplasmic reticulum membranes, but calmodulin (either form), bound to RYR1 prior to tryptic digestion, protects both the apocalmodulin and Ca2+ calmodulin sites from tryptic destruction. The protected sites are after arginines 3630 and 3637 on RYR1. These studies suggest that both Ca2+ calmodulin and apocalmodulin bind to the same or overlapping regions on RYR1 and block access of trypsin to sites at amino acids 3630 and 3637. This sequence is part of a predicted Ca2+ CaM binding site of amino acids 3614−3642 [Takeshima, H., et al. (1989) Nature 339, 439−445].</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi9907431</identifier><identifier>PMID: 10387100</identifier><language>eng</language><publisher>Legacy CDMS: American Chemical Society</publisher><subject>Animals ; Apoproteins - chemistry ; Apoproteins - metabolism ; Binding Sites ; Calcium - metabolism ; Calmodulin - chemistry ; Calmodulin - metabolism ; Hydrolysis ; Life Sciences (General) ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - metabolism ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Ryanodine Receptor Calcium Release Channel - chemistry ; Ryanodine Receptor Calcium Release Channel - metabolism ; Space life sciences ; Sulfur Radioisotopes ; Trypsin - metabolism</subject><ispartof>Biochemistry (Easton), 1999-06, Vol.38 (26), p.8532-8537</ispartof><rights>Copyright © 1999 American Chemical Society</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://pubs.acs.org/doi/pdf/10.1021/bi9907431$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi9907431$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10387100$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moore, Catherine Porter</creatorcontrib><creatorcontrib>Rodney, George</creatorcontrib><creatorcontrib>Zhang, Jia-Zheng</creatorcontrib><creatorcontrib>Santacruz-Toloza, Lucia</creatorcontrib><creatorcontrib>Strasburg, Gale</creatorcontrib><creatorcontrib>Hamilton, Susan L</creatorcontrib><title>Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The skeletal muscle Ca2+ release channel (RYR1) is regulated by calmodulin in both its Ca2+-free (apocalmodulin) and Ca2+-bound (Ca2+ calmodulin) states. Apocalmodulin is an activator of the channel, and Ca2+ calmodulin is an inhibitor of the channel. Both apocalmodulin and Ca2+ calmodulin binding sites on RYR1 are destroyed by a mild tryptic digestion of the sarcoplasmic reticulum membranes, but calmodulin (either form), bound to RYR1 prior to tryptic digestion, protects both the apocalmodulin and Ca2+ calmodulin sites from tryptic destruction. The protected sites are after arginines 3630 and 3637 on RYR1. These studies suggest that both Ca2+ calmodulin and apocalmodulin bind to the same or overlapping regions on RYR1 and block access of trypsin to sites at amino acids 3630 and 3637. This sequence is part of a predicted Ca2+ CaM binding site of amino acids 3614−3642 [Takeshima, H., et al. (1989) Nature 339, 439−445].</description><subject>Animals</subject><subject>Apoproteins - chemistry</subject><subject>Apoproteins - metabolism</subject><subject>Binding Sites</subject><subject>Calcium - metabolism</subject><subject>Calmodulin - chemistry</subject><subject>Calmodulin - metabolism</subject><subject>Hydrolysis</subject><subject>Life Sciences (General)</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Ryanodine Receptor Calcium Release Channel - chemistry</subject><subject>Ryanodine Receptor Calcium Release Channel - metabolism</subject><subject>Space life sciences</subject><subject>Sulfur Radioisotopes</subject><subject>Trypsin - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNo9kctPxCAQxonR6Po4eDemF72YKpS-OOrGZ3TV9XkjU5jVrpSupU30v5e1ugmBzDe_geEbQrYZPWQ0YkdFKQTNYs6WyIAlEQ1jIZJlMqCUpmEkUrpG1p2b-jD22CpZY5TnGaN0QPB4ViswVa07U9oArA6GEB34baGdlF5s66B9x-ABKgzG-FbWNvDrV_pAgy2Y4KZzymBfPvYaOB-8g7VoNsnKBIzDrb9zgzydnT4OL8Lr2_PL4fF1CJGI25CJbKKRFvPW8ihJ_a8gYb5TUXAdgdJ0ggp1miqVJzpnoIoCCtRccyEAc75B9vt7Z0392aFrZVU6hcaAxbpzMhW5t4czD-7-gV1RoZazpqyg-Zb_xnhgpwcsOJC2bZyM5vaxmAkW-3TYp0vX4teiHJoPmWY8S-Tj3YN8eaUvz1f3Izny_F7Pg3JyWneN9Tb41-R8fnIxP_4DMaWGXQ</recordid><startdate>19990629</startdate><enddate>19990629</enddate><creator>Moore, Catherine Porter</creator><creator>Rodney, George</creator><creator>Zhang, Jia-Zheng</creator><creator>Santacruz-Toloza, Lucia</creator><creator>Strasburg, Gale</creator><creator>Hamilton, Susan L</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CYE</scope><scope>CYI</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19990629</creationdate><title>Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel</title><author>Moore, Catherine Porter ; Rodney, George ; Zhang, Jia-Zheng ; Santacruz-Toloza, Lucia ; Strasburg, Gale ; Hamilton, Susan L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a294t-197fde0b71008256990a518719b3d2acd0feced66cc85d81acbbabed3d399ae83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Apoproteins - chemistry</topic><topic>Apoproteins - metabolism</topic><topic>Binding Sites</topic><topic>Calcium - metabolism</topic><topic>Calmodulin - chemistry</topic><topic>Calmodulin - metabolism</topic><topic>Hydrolysis</topic><topic>Life Sciences (General)</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Ryanodine Receptor Calcium Release Channel - chemistry</topic><topic>Ryanodine Receptor Calcium Release Channel - metabolism</topic><topic>Space life sciences</topic><topic>Sulfur Radioisotopes</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moore, Catherine Porter</creatorcontrib><creatorcontrib>Rodney, George</creatorcontrib><creatorcontrib>Zhang, Jia-Zheng</creatorcontrib><creatorcontrib>Santacruz-Toloza, Lucia</creatorcontrib><creatorcontrib>Strasburg, Gale</creatorcontrib><creatorcontrib>Hamilton, Susan L</creatorcontrib><collection>Istex</collection><collection>NASA Scientific and Technical Information</collection><collection>NASA Technical Reports Server</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moore, Catherine Porter</au><au>Rodney, George</au><au>Zhang, Jia-Zheng</au><au>Santacruz-Toloza, Lucia</au><au>Strasburg, Gale</au><au>Hamilton, Susan L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1999-06-29</date><risdate>1999</risdate><volume>38</volume><issue>26</issue><spage>8532</spage><epage>8537</epage><pages>8532-8537</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The skeletal muscle Ca2+ release channel (RYR1) is regulated by calmodulin in both its Ca2+-free (apocalmodulin) and Ca2+-bound (Ca2+ calmodulin) states. Apocalmodulin is an activator of the channel, and Ca2+ calmodulin is an inhibitor of the channel. Both apocalmodulin and Ca2+ calmodulin binding sites on RYR1 are destroyed by a mild tryptic digestion of the sarcoplasmic reticulum membranes, but calmodulin (either form), bound to RYR1 prior to tryptic digestion, protects both the apocalmodulin and Ca2+ calmodulin sites from tryptic destruction. The protected sites are after arginines 3630 and 3637 on RYR1. These studies suggest that both Ca2+ calmodulin and apocalmodulin bind to the same or overlapping regions on RYR1 and block access of trypsin to sites at amino acids 3630 and 3637. This sequence is part of a predicted Ca2+ CaM binding site of amino acids 3614−3642 [Takeshima, H., et al. (1989) Nature 339, 439−445].</abstract><cop>Legacy CDMS</cop><pub>American Chemical Society</pub><pmid>10387100</pmid><doi>10.1021/bi9907431</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; NASA Technical Reports Server; American Chemical Society Journals |
| subjects | Animals Apoproteins - chemistry Apoproteins - metabolism Binding Sites Calcium - metabolism Calmodulin - chemistry Calmodulin - metabolism Hydrolysis Life Sciences (General) Muscle, Skeletal - chemistry Muscle, Skeletal - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Ryanodine Receptor Calcium Release Channel - chemistry Ryanodine Receptor Calcium Release Channel - metabolism Space life sciences Sulfur Radioisotopes Trypsin - metabolism |
| title | Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel |
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