Neck-motor interactions trigger rotation of the kinesin stalk
Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that rele...
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| Veröffentlicht in: | Sci. Rep 2012-01, Vol.2 (1), p.236-236, Article 236 |
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| creator | Liu, Hong-Lei Pemble IV, Charles W. Endow, Sharyn A. |
| description | Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated – neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation – the force-producing stroke – to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states. |
| doi_str_mv | 10.1038/srep00236 |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated – neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation – the force-producing stroke – to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep00236</identifier><identifier>PMID: 22355749</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/607 ; 631/45/607/731 ; Adenosine diphosphate ; Affinity ; Crystal structure ; Crystallography, X-Ray ; Humanities and Social Sciences ; Kinesin ; Kinesins - chemistry ; Kinesins - metabolism ; Kinesins - physiology ; Kinetics ; Microtubules ; Microtubules - metabolism ; Models, Molecular ; Motor task performance ; multidisciplinary ; Neck ; Science ; Stroke</subject><ispartof>Sci. Rep, 2012-01, Vol.2 (1), p.236-236, Article 236</ispartof><rights>The Author(s) 2012</rights><rights>Copyright Nature Publishing Group Jan 2012</rights><rights>Copyright © 2012, Macmillan Publishers Limited. All rights reserved 2012 Macmillan Publishers Limited. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-9753132b97296ed88917f17cf99abf6e7b106e59a7f5461ce4aed9802fd7454b3</citedby><cites>FETCH-LOGICAL-c530t-9753132b97296ed88917f17cf99abf6e7b106e59a7f5461ce4aed9802fd7454b3</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/PMC3266953/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3266953/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22355749$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1076598$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Hong-Lei</creatorcontrib><creatorcontrib>Pemble IV, Charles W.</creatorcontrib><creatorcontrib>Endow, Sharyn A.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Neck-motor interactions trigger rotation of the kinesin stalk</title><title>Sci. Rep</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated – neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released and alter motor affinity for microtubules. 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Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.</description><subject>631/45/607</subject><subject>631/45/607/731</subject><subject>Adenosine diphosphate</subject><subject>Affinity</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Humanities and Social Sciences</subject><subject>Kinesin</subject><subject>Kinesins - chemistry</subject><subject>Kinesins - metabolism</subject><subject>Kinesins - physiology</subject><subject>Kinetics</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Models, Molecular</subject><subject>Motor task performance</subject><subject>multidisciplinary</subject><subject>Neck</subject><subject>Science</subject><subject>Stroke</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNplkU1LXDEUhkNRqowu-gfKxS6kwq35zs1CQaStBdGNXYfczLkzce4k0yQj9N83MnYYNZuEnIf3nORB6BPB3whm3XlOsMKYMvkBHVLMRUsZpXs75wN0nPMjrktQzYn-iA4oZUIorg_RxR24RbuMJabGhwLJuuJjyE1JfjaD1KRY7PNNE4emzKFZ-ADZhyYXOy6O0P5gxwzHL_sE_f7x_eH6pr29__nr-uq2dYLh0molGGG014pqCdOu00QNRLlBa9sPElRPsAShrRoEl8QBtzDVHabDVHHBezZBl5vc1bpfwtRBKMmOZpX80qa_JlpvXleCn5tZfDKMSqkFqwEnm4CYizfZ-QJu7mII4IohWEmhuwqdvnRJ8c8acjFLnx2Mow0Q19loyogmddRKfnlDPsZ1CvULDOm04phIzCv1dUO5FHPVNGwHJtg8uzNbd5X9vPvCLfnfVAXONkCupVDN7LR8l_YPezKiKA</recordid><startdate>20120127</startdate><enddate>20120127</enddate><creator>Liu, Hong-Lei</creator><creator>Pemble IV, Charles W.</creator><creator>Endow, Sharyn A.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</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>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20120127</creationdate><title>Neck-motor interactions trigger rotation of the kinesin stalk</title><author>Liu, Hong-Lei ; Pemble IV, Charles W. ; Endow, Sharyn A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-9753132b97296ed88917f17cf99abf6e7b106e59a7f5461ce4aed9802fd7454b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>631/45/607</topic><topic>631/45/607/731</topic><topic>Adenosine diphosphate</topic><topic>Affinity</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Humanities and Social Sciences</topic><topic>Kinesin</topic><topic>Kinesins - chemistry</topic><topic>Kinesins - metabolism</topic><topic>Kinesins - physiology</topic><topic>Kinetics</topic><topic>Microtubules</topic><topic>Microtubules - metabolism</topic><topic>Models, Molecular</topic><topic>Motor task performance</topic><topic>multidisciplinary</topic><topic>Neck</topic><topic>Science</topic><topic>Stroke</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Hong-Lei</creatorcontrib><creatorcontrib>Pemble IV, Charles W.</creatorcontrib><creatorcontrib>Endow, Sharyn A.</creatorcontrib><creatorcontrib>Argonne National Lab. 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Rep</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Hong-Lei</au><au>Pemble IV, Charles W.</au><au>Endow, Sharyn A.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neck-motor interactions trigger rotation of the kinesin stalk</atitle><jtitle>Sci. Rep</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2012-01-27</date><risdate>2012</risdate><volume>2</volume><issue>1</issue><spage>236</spage><epage>236</epage><pages>236-236</pages><artnum>236</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated – neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation – the force-producing stroke – to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>22355749</pmid><doi>10.1038/srep00236</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/45/607 631/45/607/731 Adenosine diphosphate Affinity Crystal structure Crystallography, X-Ray Humanities and Social Sciences Kinesin Kinesins - chemistry Kinesins - metabolism Kinesins - physiology Kinetics Microtubules Microtubules - metabolism Models, Molecular Motor task performance multidisciplinary Neck Science Stroke |
| title | Neck-motor interactions trigger rotation of the kinesin stalk |
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