A single amino acid gates the KcsA channel
•pH-dependent gating of the KcsA channel is regulated by the CPD.•E146 is the most essential amino acid for pH sensing by the KcsA.•The protonated-mimicking mutant, E146Q, is constitutively open independent of pH.•Minimal rearrangement of the CPD is sufficient for opening of the KcsA. The KcsA chann...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2014-08, Vol.450 (4), p.1537-1540 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Hirano, Minako Okuno, Daichi Onishi, Yukiko Ide, Toru |
| description | •pH-dependent gating of the KcsA channel is regulated by the CPD.•E146 is the most essential amino acid for pH sensing by the KcsA.•The protonated-mimicking mutant, E146Q, is constitutively open independent of pH.•Minimal rearrangement of the CPD is sufficient for opening of the KcsA.
The KcsA channel is a proton-activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel. |
| doi_str_mv | 10.1016/j.bbrc.2014.07.032 |
| format | Article |
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The KcsA channel is a proton-activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2014.07.032</identifier><identifier>PMID: 25019991</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; AMINO ACIDS ; CYTOPLASM ; Hydrogen-Ion Concentration ; Ion channel ; Ion Channel Gating ; IONS ; KcsA channel ; Microscopy, Fluorescence ; Mutagenesis, Site-Directed ; MUTANTS ; MUTATIONS ; PH VALUE ; pH-dependent gating ; POTASSIUM ; Potassium Channels - genetics ; Potassium Channels - physiology ; PROTONS ; Rearrangement ; SENSORS ; Single-channel recording</subject><ispartof>Biochemical and biophysical research communications, 2014-08, Vol.450 (4), p.1537-1540</ispartof><rights>2014 Elsevier Inc.</rights><rights>Copyright © 2014 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-e85c513113a50b288c764157ff78e5900d1ef48f499e3175b87df40358f5d81c3</citedby><cites>FETCH-LOGICAL-c428t-e85c513113a50b288c764157ff78e5900d1ef48f499e3175b87df40358f5d81c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2014.07.032$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25019991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22416696$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Hirano, Minako</creatorcontrib><creatorcontrib>Okuno, Daichi</creatorcontrib><creatorcontrib>Onishi, Yukiko</creatorcontrib><creatorcontrib>Ide, Toru</creatorcontrib><title>A single amino acid gates the KcsA channel</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>•pH-dependent gating of the KcsA channel is regulated by the CPD.•E146 is the most essential amino acid for pH sensing by the KcsA.•The protonated-mimicking mutant, E146Q, is constitutively open independent of pH.•Minimal rearrangement of the CPD is sufficient for opening of the KcsA.
The KcsA channel is a proton-activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>AMINO ACIDS</subject><subject>CYTOPLASM</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ion channel</subject><subject>Ion Channel Gating</subject><subject>IONS</subject><subject>KcsA channel</subject><subject>Microscopy, Fluorescence</subject><subject>Mutagenesis, Site-Directed</subject><subject>MUTANTS</subject><subject>MUTATIONS</subject><subject>PH VALUE</subject><subject>pH-dependent gating</subject><subject>POTASSIUM</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - physiology</subject><subject>PROTONS</subject><subject>Rearrangement</subject><subject>SENSORS</subject><subject>Single-channel recording</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AURQdRbK3-ARcScCNC4nuTmWQG3JTiFxbcKLgbkslLOyVNaiYV_PcmRF26uptzL5fD2DlChIDJzSbK89ZGHFBEkEYQ8wM2RdAQcgRxyKYAkIRc4_uEnXi_AUAUiT5mEy4BtdY4ZdfzwLt6VVGQbV3dBJl1RbDKOvJBt6bg2fp5YNdZXVN1yo7KrPJ09pMz9nZ_97p4DJcvD0-L-TK0gqsuJCWtxBgxziTkXCmbJgJlWpapIqkBCqRSqFJoTTGmMldpUQqIpSplodDGM3Y57ja-c8Zb15Fd26a_YDvDucAk0UlPXY3Urm0-9uQ7s3XeUlVlNTV7b1DKOAUVo-hRPqK2bbxvqTS71m2z9ssgmMGk2ZjBpBlMGkhNb7IvXfzs7_MtFX-VX3U9cDsC1Lv4dNQOV6m2VLh2eFo07r_9b4CmgFQ</recordid><startdate>20140808</startdate><enddate>20140808</enddate><creator>Hirano, Minako</creator><creator>Okuno, Daichi</creator><creator>Onishi, Yukiko</creator><creator>Ide, Toru</creator><general>Elsevier Inc</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>OTOTI</scope></search><sort><creationdate>20140808</creationdate><title>A single amino acid gates the KcsA channel</title><author>Hirano, Minako ; Okuno, Daichi ; Onishi, Yukiko ; Ide, Toru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-e85c513113a50b288c764157ff78e5900d1ef48f499e3175b87df40358f5d81c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>AMINO ACIDS</topic><topic>CYTOPLASM</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ion channel</topic><topic>Ion Channel Gating</topic><topic>IONS</topic><topic>KcsA channel</topic><topic>Microscopy, Fluorescence</topic><topic>Mutagenesis, Site-Directed</topic><topic>MUTANTS</topic><topic>MUTATIONS</topic><topic>PH VALUE</topic><topic>pH-dependent gating</topic><topic>POTASSIUM</topic><topic>Potassium Channels - genetics</topic><topic>Potassium Channels - physiology</topic><topic>PROTONS</topic><topic>Rearrangement</topic><topic>SENSORS</topic><topic>Single-channel recording</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirano, Minako</creatorcontrib><creatorcontrib>Okuno, Daichi</creatorcontrib><creatorcontrib>Onishi, Yukiko</creatorcontrib><creatorcontrib>Ide, Toru</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>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirano, Minako</au><au>Okuno, Daichi</au><au>Onishi, Yukiko</au><au>Ide, Toru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A single amino acid gates the KcsA channel</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2014-08-08</date><risdate>2014</risdate><volume>450</volume><issue>4</issue><spage>1537</spage><epage>1540</epage><pages>1537-1540</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>•pH-dependent gating of the KcsA channel is regulated by the CPD.•E146 is the most essential amino acid for pH sensing by the KcsA.•The protonated-mimicking mutant, E146Q, is constitutively open independent of pH.•Minimal rearrangement of the CPD is sufficient for opening of the KcsA.
The KcsA channel is a proton-activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>25019991</pmid><doi>10.1016/j.bbrc.2014.07.032</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2014-08, Vol.450 (4), p.1537-1540 |
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| subjects | 60 APPLIED LIFE SCIENCES AMINO ACIDS CYTOPLASM Hydrogen-Ion Concentration Ion channel Ion Channel Gating IONS KcsA channel Microscopy, Fluorescence Mutagenesis, Site-Directed MUTANTS MUTATIONS PH VALUE pH-dependent gating POTASSIUM Potassium Channels - genetics Potassium Channels - physiology PROTONS Rearrangement SENSORS Single-channel recording |
| title | A single amino acid gates the KcsA channel |
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