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Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel
Voltage-gated ion channels underlie the generation of action potentials and trigger neurosecretion and muscle contraction. These channels consist of an inner pore-forming domain, which contains the ion permeation pathway and elements of its gates, together with four voltage-sensing domains, which re...
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| Published in: | Nature (London) 1999-12, Vol.402 (6763), p.813-817 |
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| cites | cdi_FETCH-LOGICAL-c489t-2d67db195951c8e621f0a795f10fa9a2d4c089cfcd0075fe4b373222d00d18f73 |
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| container_issue | 6763 |
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| creator | Glauner, K. S. Mannuzzu, L. M. Gandhi, C. S. Isacoff, E. Y. |
| description | Voltage-gated ion channels underlie the generation of action potentials and trigger neurosecretion and muscle contraction. These channels consist of an inner pore-forming domain, which contains the ion permeation pathway and elements of its gates, together with four voltage-sensing domains, which regulate the gates
1
,
2
,
3
,
4
,
5
,
6
. To understand the mechanism of voltage sensing it is necessary to define the structure and motion of the S4 segment, the portion of each voltage-sensing domain that moves charged residues across the membrane in response to voltage change
7
,
8
,
9
,
10
,
11
,
12
,
13
,
14
. We have addressed this problem by using fluorescence resonance energy transfer as a spectroscopic ruler
15
,
16
,
17
to determine distances between S4s in the
Shaker
K
+
channel in different gating states. Here we provide evidence consistent with S4 being a tilted helix that twists during activation. We propose that helical twist contributes to the movement of charged side chains across the membrane electric field and that it is involved in coupling voltage sensing to gating. |
| doi_str_mv | 10.1038/45561 |
| format | article |
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1
,
2
,
3
,
4
,
5
,
6
. To understand the mechanism of voltage sensing it is necessary to define the structure and motion of the S4 segment, the portion of each voltage-sensing domain that moves charged residues across the membrane in response to voltage change
7
,
8
,
9
,
10
,
11
,
12
,
13
,
14
. We have addressed this problem by using fluorescence resonance energy transfer as a spectroscopic ruler
15
,
16
,
17
to determine distances between S4s in the
Shaker
K
+
channel in different gating states. Here we provide evidence consistent with S4 being a tilted helix that twists during activation. We propose that helical twist contributes to the movement of charged side chains across the membrane electric field and that it is involved in coupling voltage sensing to gating.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/45561</identifier><identifier>PMID: 10617202</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Biological and medical sciences ; Cell membranes. Ionic channels. Membrane pores ; Cell structures and functions ; Electrochemistry ; Energy transfer ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Ion Channel Gating ; letter ; Molecular and cellular biology ; multidisciplinary ; Mutagenesis, Site-Directed ; Physics ; Potassium Channels - chemistry ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Protein Conformation ; Resonance ; Science ; Science (multidisciplinary) ; Shaker Superfamily of Potassium Channels ; Spectrometry, Fluorescence - methods ; Spectrum analysis ; Xenopus</subject><ispartof>Nature (London), 1999-12, Vol.402 (6763), p.813-817</ispartof><rights>Macmillan Magazines Ltd. 1999</rights><rights>2000 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Dec 16, 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c489t-2d67db195951c8e621f0a795f10fa9a2d4c089cfcd0075fe4b373222d00d18f73</citedby><cites>FETCH-LOGICAL-c489t-2d67db195951c8e621f0a795f10fa9a2d4c089cfcd0075fe4b373222d00d18f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1332276$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10617202$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Glauner, K. S.</creatorcontrib><creatorcontrib>Mannuzzu, L. M.</creatorcontrib><creatorcontrib>Gandhi, C. S.</creatorcontrib><creatorcontrib>Isacoff, E. Y.</creatorcontrib><title>Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Voltage-gated ion channels underlie the generation of action potentials and trigger neurosecretion and muscle contraction. These channels consist of an inner pore-forming domain, which contains the ion permeation pathway and elements of its gates, together with four voltage-sensing domains, which regulate the gates
1
,
2
,
3
,
4
,
5
,
6
. To understand the mechanism of voltage sensing it is necessary to define the structure and motion of the S4 segment, the portion of each voltage-sensing domain that moves charged residues across the membrane in response to voltage change
7
,
8
,
9
,
10
,
11
,
12
,
13
,
14
. We have addressed this problem by using fluorescence resonance energy transfer as a spectroscopic ruler
15
,
16
,
17
to determine distances between S4s in the
Shaker
K
+
channel in different gating states. Here we provide evidence consistent with S4 being a tilted helix that twists during activation. We propose that helical twist contributes to the movement of charged side chains across the membrane electric field and that it is involved in coupling voltage sensing to gating.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell membranes. Ionic channels. Membrane pores</subject><subject>Cell structures and functions</subject><subject>Electrochemistry</subject><subject>Energy transfer</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Ion Channel Gating</subject><subject>letter</subject><subject>Molecular and cellular biology</subject><subject>multidisciplinary</subject><subject>Mutagenesis, Site-Directed</subject><subject>Physics</subject><subject>Potassium Channels - chemistry</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - metabolism</subject><subject>Protein Conformation</subject><subject>Resonance</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Shaker Superfamily of Potassium Channels</subject><subject>Spectrometry, Fluorescence - methods</subject><subject>Spectrum analysis</subject><subject>Xenopus</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNp90d9rFDEQB_AgFnvW_gsSRO3T6iSbX_sopdVCoUL1ecllJ3dbd5M12S30v2_aOzj1wacQ8mEy8x1CThl8YlCbz0JKxV6QFRNaVUIZ_ZKsALipwNTqmLzO-Q4AJNPiFTlmoJjmwFfk--2Ebk4xuzj1jo52mvqwodHT-zjMdoM0Y8gx0THe44hhpn2g8xbp7db-wkSnONuc-2WkbmtDwOENOfJ2yHi6P0_Iz8uLH-ffquubr1fnX64rJ0wzV7xTuluzRjaSOYOKMw9WN9Iz8LaxvBMOTOO86wC09CjWta455-XaMeN1fULOdnWnFH8vmOd27LPDYbAB45JbLWota2F4kR__K0skXHD1BN_9A-_ikkKZouUghJLqGX3YIVdCywl9O6V-tOmhZdA-baJ93kRxb_fFlvWI3R9qF30B7_fAZmcHn2xwfT64uoyr1aH7XF7CBtOhqb8_fAQCvppL</recordid><startdate>19991216</startdate><enddate>19991216</enddate><creator>Glauner, K. 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S.</au><au>Mannuzzu, L. M.</au><au>Gandhi, C. S.</au><au>Isacoff, E. Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1999-12-16</date><risdate>1999</risdate><volume>402</volume><issue>6763</issue><spage>813</spage><epage>817</epage><pages>813-817</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Voltage-gated ion channels underlie the generation of action potentials and trigger neurosecretion and muscle contraction. These channels consist of an inner pore-forming domain, which contains the ion permeation pathway and elements of its gates, together with four voltage-sensing domains, which regulate the gates
1
,
2
,
3
,
4
,
5
,
6
. To understand the mechanism of voltage sensing it is necessary to define the structure and motion of the S4 segment, the portion of each voltage-sensing domain that moves charged residues across the membrane in response to voltage change
7
,
8
,
9
,
10
,
11
,
12
,
13
,
14
. We have addressed this problem by using fluorescence resonance energy transfer as a spectroscopic ruler
15
,
16
,
17
to determine distances between S4s in the
Shaker
K
+
channel in different gating states. Here we provide evidence consistent with S4 being a tilted helix that twists during activation. We propose that helical twist contributes to the movement of charged side chains across the membrane electric field and that it is involved in coupling voltage sensing to gating.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>10617202</pmid><doi>10.1038/45561</doi><tpages>5</tpages></addata></record> |
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| ispartof | Nature (London), 1999-12, Vol.402 (6763), p.813-817 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743753482 |
| source | Single Title from Nature Journals |
| subjects | Animals Biological and medical sciences Cell membranes. Ionic channels. Membrane pores Cell structures and functions Electrochemistry Energy transfer Fluorescence Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Ion Channel Gating letter Molecular and cellular biology multidisciplinary Mutagenesis, Site-Directed Physics Potassium Channels - chemistry Potassium Channels - genetics Potassium Channels - metabolism Protein Conformation Resonance Science Science (multidisciplinary) Shaker Superfamily of Potassium Channels Spectrometry, Fluorescence - methods Spectrum analysis Xenopus |
| title | Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel |
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