Complex Voltage-Dependent Behavior of Single Unliganded Calcium-Sensitive Potassium Channels
The study and characterization of unliganded openings is of central significance for the elucidation of gating mechanisms for allosteric ligand-gated ion channels. Unliganded openings have been reported for many channel types, but their low open probability can make it difficult to study their kinet...
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| Veröffentlicht in: | Biophysical journal 2000-02, Vol.78 (2), p.761-772 |
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| description | The study and characterization of unliganded openings is of central significance for the elucidation of gating mechanisms for allosteric ligand-gated ion channels. Unliganded openings have been reported for many channel types, but their low open probability can make it difficult to study their kinetics in detail. Because the large conductance calcium-activated potassium channel
mSlo is sensitive to both intracellular calcium and to membrane potential, we have been able to obtain stable unliganded single-channel recordings of
mSlo with relatively high opening probability. We have found that the single-channel gating behavior of
mSlo is complex, with multiple open and closed states, even when no ligand is present. Our results rule out a Monod–Wyman–Changeux allosteric mechanism with a central voltage-dependent concerted step, and they support the existence of quaternary states with less than the full number of voltage sensors activated, as has been suggested by previous work involving measurements of gating currents. |
| doi_str_mv | 10.1016/S0006-3495(00)76634-3 |
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mSlo is sensitive to both intracellular calcium and to membrane potential, we have been able to obtain stable unliganded single-channel recordings of
mSlo with relatively high opening probability. We have found that the single-channel gating behavior of
mSlo is complex, with multiple open and closed states, even when no ligand is present. Our results rule out a Monod–Wyman–Changeux allosteric mechanism with a central voltage-dependent concerted step, and they support the existence of quaternary states with less than the full number of voltage sensors activated, as has been suggested by previous work involving measurements of gating currents.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(00)76634-3</identifier><identifier>PMID: 10653789</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Calcium - metabolism ; Electrophysiology ; Ion Channel Gating ; Kinetics ; Large-Conductance Calcium-Activated Potassium Channels ; Ligands ; Mice ; Models, Biological ; Potassium Channels - metabolism ; Potassium Channels, Calcium-Activated</subject><ispartof>Biophysical journal, 2000-02, Vol.78 (2), p.761-772</ispartof><rights>2000 The Biophysical Society</rights><rights>Copyright Biophysical Society Feb 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-3bbfb356ea51e0704777a338216fe85472dcfde387cab16d3bc58520e6589ef73</citedby><cites>FETCH-LOGICAL-c490t-3bbfb356ea51e0704777a338216fe85472dcfde387cab16d3bc58520e6589ef73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1300679/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(00)76634-3$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3548,27923,27924,45994,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10653789$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Talukder, Gargi</creatorcontrib><creatorcontrib>Aldrich, Richard W.</creatorcontrib><title>Complex Voltage-Dependent Behavior of Single Unliganded Calcium-Sensitive Potassium Channels</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The study and characterization of unliganded openings is of central significance for the elucidation of gating mechanisms for allosteric ligand-gated ion channels. Unliganded openings have been reported for many channel types, but their low open probability can make it difficult to study their kinetics in detail. Because the large conductance calcium-activated potassium channel
mSlo is sensitive to both intracellular calcium and to membrane potential, we have been able to obtain stable unliganded single-channel recordings of
mSlo with relatively high opening probability. We have found that the single-channel gating behavior of
mSlo is complex, with multiple open and closed states, even when no ligand is present. Our results rule out a Monod–Wyman–Changeux allosteric mechanism with a central voltage-dependent concerted step, and they support the existence of quaternary states with less than the full number of voltage sensors activated, as has been suggested by previous work involving measurements of gating currents.</description><subject>Animals</subject><subject>Calcium - metabolism</subject><subject>Electrophysiology</subject><subject>Ion Channel Gating</subject><subject>Kinetics</subject><subject>Large-Conductance Calcium-Activated Potassium Channels</subject><subject>Ligands</subject><subject>Mice</subject><subject>Models, Biological</subject><subject>Potassium Channels - metabolism</subject><subject>Potassium Channels, Calcium-Activated</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkU1v1DAQhi0EokvhJ4AiDqgcAuM4tpNLEQ2fUiWQlnJCshxnsuvKsRc7WcG_x-1WVeHCaaSZZ975eAl5SuEVBSperwFAlKxu-QnASykEq0t2j6wor6sSoBH3yeoWOSKPUroEoBUH-pAcURCcyaZdkR9dmHYOfxXfg5v1Bst3uEM_oJ-LM9zqvQ2xCGOxtn7jsLjwzm50Lg9Fp52xy1Su0Sc72z0WX8OsU8q5ottq79Glx-TBqF3CJzfxmFx8eP-t-1Sef_n4uXt7Xpq6hblkfT_2jAvUnCJIqKWUmrGmomLEhteyGsw4IGuk0T0VA-sNb3gFKHjT4ijZMTk96O6WfsLB5O2jdmoX7aTjbxW0VX9XvN2qTdgryvKHZJsFXtwIxPBzwTSrySaDzmmPYUlKQtNSWdUZfP4PeBmW6PNxqqJcVpRxmiF-gEwMKUUcbzehoK7MU9fmqStnFIC6Nk-x3Pfs7hl3ug5uZeDNAci_xb3FqJKx6A0ONqKZ1RDsf0b8AUoXqpc</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Talukder, Gargi</creator><creator>Aldrich, Richard W.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000201</creationdate><title>Complex Voltage-Dependent Behavior of Single Unliganded Calcium-Sensitive Potassium Channels</title><author>Talukder, Gargi ; Aldrich, Richard W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-3bbfb356ea51e0704777a338216fe85472dcfde387cab16d3bc58520e6589ef73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Calcium - metabolism</topic><topic>Electrophysiology</topic><topic>Ion Channel Gating</topic><topic>Kinetics</topic><topic>Large-Conductance Calcium-Activated Potassium Channels</topic><topic>Ligands</topic><topic>Mice</topic><topic>Models, Biological</topic><topic>Potassium Channels - metabolism</topic><topic>Potassium Channels, Calcium-Activated</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Talukder, Gargi</creatorcontrib><creatorcontrib>Aldrich, Richard W.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Talukder, Gargi</au><au>Aldrich, Richard W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complex Voltage-Dependent Behavior of Single Unliganded Calcium-Sensitive Potassium Channels</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>78</volume><issue>2</issue><spage>761</spage><epage>772</epage><pages>761-772</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The study and characterization of unliganded openings is of central significance for the elucidation of gating mechanisms for allosteric ligand-gated ion channels. Unliganded openings have been reported for many channel types, but their low open probability can make it difficult to study their kinetics in detail. Because the large conductance calcium-activated potassium channel
mSlo is sensitive to both intracellular calcium and to membrane potential, we have been able to obtain stable unliganded single-channel recordings of
mSlo with relatively high opening probability. We have found that the single-channel gating behavior of
mSlo is complex, with multiple open and closed states, even when no ligand is present. Our results rule out a Monod–Wyman–Changeux allosteric mechanism with a central voltage-dependent concerted step, and they support the existence of quaternary states with less than the full number of voltage sensors activated, as has been suggested by previous work involving measurements of gating currents.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10653789</pmid><doi>10.1016/S0006-3495(00)76634-3</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Animals Calcium - metabolism Electrophysiology Ion Channel Gating Kinetics Large-Conductance Calcium-Activated Potassium Channels Ligands Mice Models, Biological Potassium Channels - metabolism Potassium Channels, Calcium-Activated |
| title | Complex Voltage-Dependent Behavior of Single Unliganded Calcium-Sensitive Potassium Channels |
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