A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel
Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. The polarity of the side chain at position 393 determines the stability of the open state, probably by...
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| Veröffentlicht in: | Pflügers Archiv 1998-04, Vol.435 (5), p.654-661 |
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| creator | Liu, Y Joho, R H |
| description | Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. The polarity of the side chain at position 393 determines the stability of the open state, probably by interaction of S6 with the narrow part of the ion-conduction pathway; however, the substitutions at position 393 have no effect on the stability of the closed state. An increase in side-chain volume leads to greater K+ conductance; in contrast, gradual decreases in side-chain volume lead to progressively smaller K+ conductances concomitantly with larger Rb+ conductances. Although the substitutions for Cys393 alter open-state stability and ion permeation, they have no effect on block by external or internal tetraethylammonium (TEA). Our data indicate that molecular determinants that are involved in conformational transitions between the open state and the brief closed state (i.e., voltage-independent gating) and ion selectivity are located within the sphere of influence of the conserved Cys393 in S6. This region is physically separated from the voltage-controlled activation gate located on the intracellular side of the K+ channel. |
| doi_str_mv | 10.1007/s004240050566 |
| format | Article |
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The polarity of the side chain at position 393 determines the stability of the open state, probably by interaction of S6 with the narrow part of the ion-conduction pathway; however, the substitutions at position 393 have no effect on the stability of the closed state. An increase in side-chain volume leads to greater K+ conductance; in contrast, gradual decreases in side-chain volume lead to progressively smaller K+ conductances concomitantly with larger Rb+ conductances. Although the substitutions for Cys393 alter open-state stability and ion permeation, they have no effect on block by external or internal tetraethylammonium (TEA). Our data indicate that molecular determinants that are involved in conformational transitions between the open state and the brief closed state (i.e., voltage-independent gating) and ion selectivity are located within the sphere of influence of the conserved Cys393 in S6. This region is physically separated from the voltage-controlled activation gate located on the intracellular side of the K+ channel.</description><identifier>ISSN: 0031-6768</identifier><identifier>EISSN: 1432-2013</identifier><identifier>DOI: 10.1007/s004240050566</identifier><identifier>PMID: 9479018</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>Amino Acid Substitution ; Animals ; Cysteine - genetics ; Delayed Rectifier Potassium Channels ; Electric Conductivity ; Ion Channel Gating ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Permeability ; Potassium Channel Blockers ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated ; Proteins ; Shab Potassium Channels ; Tetraethylammonium - pharmacology ; Xenopus laevis</subject><ispartof>Pflügers Archiv, 1998-04, Vol.435 (5), p.654-661</ispartof><rights>Springer-Verlag Berlin Heidelberg 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c315t-66ee22c40d0c4c6fe99f78db5df124fbc6499174142ffe26cb6d1935f2694acd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27926,27927</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9479018$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Y</creatorcontrib><creatorcontrib>Joho, R H</creatorcontrib><title>A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel</title><title>Pflügers Archiv</title><addtitle>Pflugers Arch</addtitle><description>Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. The polarity of the side chain at position 393 determines the stability of the open state, probably by interaction of S6 with the narrow part of the ion-conduction pathway; however, the substitutions at position 393 have no effect on the stability of the closed state. An increase in side-chain volume leads to greater K+ conductance; in contrast, gradual decreases in side-chain volume lead to progressively smaller K+ conductances concomitantly with larger Rb+ conductances. Although the substitutions for Cys393 alter open-state stability and ion permeation, they have no effect on block by external or internal tetraethylammonium (TEA). Our data indicate that molecular determinants that are involved in conformational transitions between the open state and the brief closed state (i.e., voltage-independent gating) and ion selectivity are located within the sphere of influence of the conserved Cys393 in S6. This region is physically separated from the voltage-controlled activation gate located on the intracellular side of the K+ channel.</description><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Cysteine - genetics</subject><subject>Delayed Rectifier Potassium Channels</subject><subject>Electric Conductivity</subject><subject>Ion Channel Gating</subject><subject>Mutation</subject><subject>Oocytes</subject><subject>Patch-Clamp Techniques</subject><subject>Permeability</subject><subject>Potassium Channel Blockers</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - metabolism</subject><subject>Potassium Channels, Voltage-Gated</subject><subject>Proteins</subject><subject>Shab Potassium Channels</subject><subject>Tetraethylammonium - pharmacology</subject><subject>Xenopus laevis</subject><issn>0031-6768</issn><issn>1432-2013</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkE1LxDAQhoMouq4ePQrBgxepTtI0aY7L4hcKHtRzSZOJ26Wbrk0r7L83i4ugMMzM4ZmX4SHkjME1A1A3EUBwAVBAIeUemTCR84wDy_fJBCBnmVSyPCLHMS4BgIuSH5JDLZQGVk7IYkZj45DahWkCTfUqU_ftiMFipHU3LGi3xpDFwQxIU6-bthk21ARHmy7QNfYrNMN2TdeGfnXtYD4w-0i4o09X2-QQsD0hB960EU93c0re727f5g_Z88v943z2nNmcFUMmJSLnVoADK6z0qLVXpasL5xkXvrZSaM2UYIJ7j1zaWjqm88JzqYWxLp-Sy5_cdd99jhiHatVEi21rAnZjrJRWSZTSCbz4By67sQ_pt6pUpS6g5DJB2Q9k-y7GHn217puV6TcVg2qrv_qjP_Hnu9CxXqH7pXe-829TNX6x</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Liu, Y</creator><creator>Joho, R H</creator><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7TS</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope></search><sort><creationdate>19980401</creationdate><title>A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel</title><author>Liu, Y ; Joho, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-66ee22c40d0c4c6fe99f78db5df124fbc6499174142ffe26cb6d1935f2694acd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Cysteine - genetics</topic><topic>Delayed Rectifier Potassium Channels</topic><topic>Electric Conductivity</topic><topic>Ion Channel Gating</topic><topic>Mutation</topic><topic>Oocytes</topic><topic>Patch-Clamp Techniques</topic><topic>Permeability</topic><topic>Potassium Channel Blockers</topic><topic>Potassium Channels - genetics</topic><topic>Potassium Channels - metabolism</topic><topic>Potassium Channels, Voltage-Gated</topic><topic>Proteins</topic><topic>Shab Potassium Channels</topic><topic>Tetraethylammonium - pharmacology</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Y</creatorcontrib><creatorcontrib>Joho, R H</creatorcontrib><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>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Physical Education Index</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Biological Science Journals</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Pflügers Archiv</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Y</au><au>Joho, R H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel</atitle><jtitle>Pflügers Archiv</jtitle><addtitle>Pflugers Arch</addtitle><date>1998-04-01</date><risdate>1998</risdate><volume>435</volume><issue>5</issue><spage>654</spage><epage>661</epage><pages>654-661</pages><issn>0031-6768</issn><eissn>1432-2013</eissn><abstract>Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. The polarity of the side chain at position 393 determines the stability of the open state, probably by interaction of S6 with the narrow part of the ion-conduction pathway; however, the substitutions at position 393 have no effect on the stability of the closed state. An increase in side-chain volume leads to greater K+ conductance; in contrast, gradual decreases in side-chain volume lead to progressively smaller K+ conductances concomitantly with larger Rb+ conductances. Although the substitutions for Cys393 alter open-state stability and ion permeation, they have no effect on block by external or internal tetraethylammonium (TEA). Our data indicate that molecular determinants that are involved in conformational transitions between the open state and the brief closed state (i.e., voltage-independent gating) and ion selectivity are located within the sphere of influence of the conserved Cys393 in S6. This region is physically separated from the voltage-controlled activation gate located on the intracellular side of the K+ channel.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>9479018</pmid><doi>10.1007/s004240050566</doi><tpages>8</tpages></addata></record> |
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| issn | 0031-6768 1432-2013 |
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| source | MEDLINE; SpringerNature Journals |
| subjects | Amino Acid Substitution Animals Cysteine - genetics Delayed Rectifier Potassium Channels Electric Conductivity Ion Channel Gating Mutation Oocytes Patch-Clamp Techniques Permeability Potassium Channel Blockers Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated Proteins Shab Potassium Channels Tetraethylammonium - pharmacology Xenopus laevis |
| title | A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel |
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