FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge
Ryanodine Receptors (RyRs) are intracellular Ca 2+ channels that mediate Ca 2+ flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads t...
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| Veröffentlicht in: | Channels (Austin, Tex.) Tex.), 2017-09, Vol.11 (5), p.415-425 |
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| container_title | Channels (Austin, Tex.) |
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| creator | Gonano, Luis A. Jones, Peter P. |
| description | Ryanodine Receptors (RyRs) are intracellular Ca
2+
channels that mediate Ca
2+
flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads to channel dysfunction. In the heart, phosphorylation of RyR has been suggested to disrupt the RyR-FKBP interaction promoting altered Ca
2+
signaling, heart failure and arrhythmias. However, the functional result of FKBP interaction with RyR and how this interaction is regulated remains highly controversial. Recently, high resolution structures of RyR have provided novel aspects to the ongoing debate. This review will discuss the most recent functional data in light of these new structures. |
| doi_str_mv | 10.1080/19336950.2017.1344799 |
| format | Article |
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2+
channels that mediate Ca
2+
flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads to channel dysfunction. In the heart, phosphorylation of RyR has been suggested to disrupt the RyR-FKBP interaction promoting altered Ca
2+
signaling, heart failure and arrhythmias. However, the functional result of FKBP interaction with RyR and how this interaction is regulated remains highly controversial. Recently, high resolution structures of RyR have provided novel aspects to the ongoing debate. This review will discuss the most recent functional data in light of these new structures.</description><identifier>ISSN: 1933-6950</identifier><identifier>EISSN: 1933-6969</identifier><identifier>DOI: 10.1080/19336950.2017.1344799</identifier><identifier>PMID: 28636428</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Animals ; arrhythmias ; Arrhythmias, Cardiac - metabolism ; Calcium - metabolism ; CPVT ; FKBP ; heart failure ; Heart Failure - metabolism ; Humans ; Myocardium - metabolism ; Phosphorylation ; Protein Binding ; Review ; Ryanodine Receptor ; Ryanodine Receptor Calcium Release Channel - metabolism ; Signal Transduction ; SR Ca leak ; Tacrolimus Binding Protein 1A - metabolism</subject><ispartof>Channels (Austin, Tex.), 2017-09, Vol.11 (5), p.415-425</ispartof><rights>2017 Taylor & Francis 2017</rights><rights>2017 Taylor & Francis 2017 Taylor & Francis</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c494t-9f3844110f09cf22807a28e4489e4214fa8e3efec623ba004e6cc87813b5a7ab3</citedby><cites>FETCH-LOGICAL-c494t-9f3844110f09cf22807a28e4489e4214fa8e3efec623ba004e6cc87813b5a7ab3</cites><orcidid>0000-0001-9519-778X ; 0000-0001-7977-1737</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5626368/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5626368/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,729,782,786,887,27933,27934,53800,53802</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28636428$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gonano, Luis A.</creatorcontrib><creatorcontrib>Jones, Peter P.</creatorcontrib><title>FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge</title><title>Channels (Austin, Tex.)</title><addtitle>Channels (Austin)</addtitle><description>Ryanodine Receptors (RyRs) are intracellular Ca
2+
channels that mediate Ca
2+
flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads to channel dysfunction. In the heart, phosphorylation of RyR has been suggested to disrupt the RyR-FKBP interaction promoting altered Ca
2+
signaling, heart failure and arrhythmias. However, the functional result of FKBP interaction with RyR and how this interaction is regulated remains highly controversial. Recently, high resolution structures of RyR have provided novel aspects to the ongoing debate. This review will discuss the most recent functional data in light of these new structures.</description><subject>Animals</subject><subject>arrhythmias</subject><subject>Arrhythmias, Cardiac - metabolism</subject><subject>Calcium - metabolism</subject><subject>CPVT</subject><subject>FKBP</subject><subject>heart failure</subject><subject>Heart Failure - metabolism</subject><subject>Humans</subject><subject>Myocardium - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Review</subject><subject>Ryanodine Receptor</subject><subject>Ryanodine Receptor Calcium Release Channel - metabolism</subject><subject>Signal Transduction</subject><subject>SR Ca leak</subject><subject>Tacrolimus Binding Protein 1A - metabolism</subject><issn>1933-6950</issn><issn>1933-6969</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u1DAUhSMEoqXwCCAvyyKD_-LYLBBQMVC1EqiCteU416khY09th9G8BM9MhpmOYMPq2r7nnHvlr6qeE7wgWOJXRDEmVIMXFJN2QRjnrVIPqtPdey2UUA-P5wafVE9y_o6xYJSQx9UJlYIJTuVp9Wt51WBRdz70PgxonWIBHzIiFJnQz2Uh0Pny6v2X_BKZjBIM02hKTBlFh6xJvTcW3WxNiLMf0A1YWO_ar9FlyH64LRm5FFcowAa5KdjiYzDjn-xc0mTLlObrjxA3I_QDPK0eOTNmeHaoZ9W35YevF5_q688fLy_eXdeWK15q5ZjknBDssLKOUolbQyVwLhVwSrgzEhg4sIKyzmDMQVgrW0lY15jWdOyserPPXU_dCnoLocx76HXyK5O2Ohqv_-0Ef6uH-FM3gs5fJ-eA80NAincT5KJXPlsYRxMgTlkTRaggoqF4ljZ7qU0x5wTuOIZgvWOp71nqHUt9YDn7Xvy949F1D28WvN0LfHAxrcwmprHXxWzHmFwywfqs2f9n_AboLa87</recordid><startdate>20170903</startdate><enddate>20170903</enddate><creator>Gonano, Luis A.</creator><creator>Jones, Peter P.</creator><general>Taylor & Francis</general><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><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-9519-778X</orcidid><orcidid>https://orcid.org/0000-0001-7977-1737</orcidid></search><sort><creationdate>20170903</creationdate><title>FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge</title><author>Gonano, Luis A. ; Jones, Peter P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-9f3844110f09cf22807a28e4489e4214fa8e3efec623ba004e6cc87813b5a7ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>arrhythmias</topic><topic>Arrhythmias, Cardiac - metabolism</topic><topic>Calcium - metabolism</topic><topic>CPVT</topic><topic>FKBP</topic><topic>heart failure</topic><topic>Heart Failure - metabolism</topic><topic>Humans</topic><topic>Myocardium - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Review</topic><topic>Ryanodine Receptor</topic><topic>Ryanodine Receptor Calcium Release Channel - metabolism</topic><topic>Signal Transduction</topic><topic>SR Ca leak</topic><topic>Tacrolimus Binding Protein 1A - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gonano, Luis A.</creatorcontrib><creatorcontrib>Jones, Peter P.</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Channels (Austin, Tex.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gonano, Luis A.</au><au>Jones, Peter P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge</atitle><jtitle>Channels (Austin, Tex.)</jtitle><addtitle>Channels (Austin)</addtitle><date>2017-09-03</date><risdate>2017</risdate><volume>11</volume><issue>5</issue><spage>415</spage><epage>425</epage><pages>415-425</pages><issn>1933-6950</issn><eissn>1933-6969</eissn><abstract>Ryanodine Receptors (RyRs) are intracellular Ca
2+
channels that mediate Ca
2+
flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads to channel dysfunction. In the heart, phosphorylation of RyR has been suggested to disrupt the RyR-FKBP interaction promoting altered Ca
2+
signaling, heart failure and arrhythmias. However, the functional result of FKBP interaction with RyR and how this interaction is regulated remains highly controversial. Recently, high resolution structures of RyR have provided novel aspects to the ongoing debate. This review will discuss the most recent functional data in light of these new structures.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>28636428</pmid><doi>10.1080/19336950.2017.1344799</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-9519-778X</orcidid><orcidid>https://orcid.org/0000-0001-7977-1737</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Channels (Austin, Tex.), 2017-09, Vol.11 (5), p.415-425 |
| issn | 1933-6950 1933-6969 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Animals arrhythmias Arrhythmias, Cardiac - metabolism Calcium - metabolism CPVT FKBP heart failure Heart Failure - metabolism Humans Myocardium - metabolism Phosphorylation Protein Binding Review Ryanodine Receptor Ryanodine Receptor Calcium Release Channel - metabolism Signal Transduction SR Ca leak Tacrolimus Binding Protein 1A - metabolism |
| title | FK506-binding proteins 12 and 12.6 (FKBPs) as regulators of cardiac Ryanodine Receptors: Insights from new functional and structural knowledge |
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