A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules
The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR protein. Tandem linkage of two CFTR molecules produ...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-03, Vol.274 (12), p.7627-7630 |
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| container_issue | 12 |
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| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Zerhusen, B Zhao, J Xie, J Davis, P B Ma, J |
| description | The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated
chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR
protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those
of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance
of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with
mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together
to form a single conductance pore for chloride ions. |
| doi_str_mv | 10.1074/jbc.274.12.7627 |
| format | Article |
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chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR
protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those
of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance
of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with
mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together
to form a single conductance pore for chloride ions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.12.7627</identifier><identifier>PMID: 10075649</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate - metabolism ; Cell Line ; Chloride Channels - metabolism ; Chlorides - metabolism ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator - metabolism ; Dimerization ; Humans ; Ion Channel Gating ; Lipid Bilayers - metabolism ; Thrombin - pharmacology</subject><ispartof>The Journal of biological chemistry, 1999-03, Vol.274 (12), p.7627-7630</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-c64863563e9700c7476f1c8e9410fb31424dc5bc86cfc26dab893e4a87fe9cf23</citedby><cites>FETCH-LOGICAL-c393t-c64863563e9700c7476f1c8e9410fb31424dc5bc86cfc26dab893e4a87fe9cf23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10075649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zerhusen, B</creatorcontrib><creatorcontrib>Zhao, J</creatorcontrib><creatorcontrib>Xie, J</creatorcontrib><creatorcontrib>Davis, P B</creatorcontrib><creatorcontrib>Ma, J</creatorcontrib><title>A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated
chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR
protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those
of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance
of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with
mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together
to form a single conductance pore for chloride ions.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Cell Line</subject><subject>Chloride Channels - metabolism</subject><subject>Chlorides - metabolism</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Cystic Fibrosis Transmembrane Conductance Regulator - metabolism</subject><subject>Dimerization</subject><subject>Humans</subject><subject>Ion Channel Gating</subject><subject>Lipid Bilayers - metabolism</subject><subject>Thrombin - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9LHDEYQEOx1K323JsEBG-z5tckk6MMrhUsFV3BW5hkvtmNzEw0mWHZ_76R9VBPzeW7vDyS7yH0k5IlJUpcvli3ZEosKVsqydQXtKCk4gUv6fMRWhDCaKFZWR2j7ym9kHyEpt_QMSVElVLoBdpd4Uc_bnrAdRjb2U3N6ADfhwi4CxHX2z5E3wK-DWPCqxAHaLHd4_Uu4HqfJu_wytsYkk94HZsxDTDYPD_rHmAz982Ufb9DD27uIZ2ir13TJ_jxMU_Q0-p6Xf8q7v7c3NZXd4Xjmk-Fk6KSvJQctCLEKaFkR10FWlDSWU4FE60rrauk6xyTbWMrzUE0lepAu47xE3Rx8L7G8DZDmszgk4O-z28MczJSSyaY5v8FqaJKM1Jm8PIAuvztFKEzr9EPTdwbSsx7FJOjmBzFUGbeo-QbZx_q2eb9_cMfKmTg_ABs_Wa78xGM9cFtYfik-Qv5BJSi</recordid><startdate>19990319</startdate><enddate>19990319</enddate><creator>Zerhusen, B</creator><creator>Zhao, J</creator><creator>Xie, J</creator><creator>Davis, P B</creator><creator>Ma, J</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19990319</creationdate><title>A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules</title><author>Zerhusen, B ; Zhao, J ; Xie, J ; Davis, P B ; Ma, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-c64863563e9700c7476f1c8e9410fb31424dc5bc86cfc26dab893e4a87fe9cf23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Cell Line</topic><topic>Chloride Channels - metabolism</topic><topic>Chlorides - metabolism</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Cystic Fibrosis Transmembrane Conductance Regulator - metabolism</topic><topic>Dimerization</topic><topic>Humans</topic><topic>Ion Channel Gating</topic><topic>Lipid Bilayers - metabolism</topic><topic>Thrombin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zerhusen, B</creatorcontrib><creatorcontrib>Zhao, J</creatorcontrib><creatorcontrib>Xie, J</creatorcontrib><creatorcontrib>Davis, P B</creatorcontrib><creatorcontrib>Ma, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zerhusen, B</au><au>Zhao, J</au><au>Xie, J</au><au>Davis, P B</au><au>Ma, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-03-19</date><risdate>1999</risdate><volume>274</volume><issue>12</issue><spage>7627</spage><epage>7630</epage><pages>7627-7630</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated
chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR
protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those
of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance
of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with
mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together
to form a single conductance pore for chloride ions.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10075649</pmid><doi>10.1074/jbc.274.12.7627</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1999-03, Vol.274 (12), p.7627-7630 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69624293 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Cell Line Chloride Channels - metabolism Chlorides - metabolism Cyclic AMP-Dependent Protein Kinases - metabolism Cystic Fibrosis Transmembrane Conductance Regulator - metabolism Dimerization Humans Ion Channel Gating Lipid Bilayers - metabolism Thrombin - pharmacology |
| title | A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules |
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