Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI
Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made po...
Gespeichert in:
| Veröffentlicht in: | Nature structural & molecular biology 2008-09, Vol.15 (6), p.591 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 6 |
| container_start_page | 591 |
| container_title | Nature structural & molecular biology |
| container_volume | 15 |
| creator | Spink, Benjamin J Sivaramakrishnan, Sivaraj Lipfert, Jan Doniach, Sebastian Spudich, James A |
| description | Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of approximately 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the approximately 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization. [PUBLICATION ABSTRACT] |
| doi_str_mv | 10.1038/nsmb.1429 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_1006723</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1492367421</sourcerecordid><originalsourceid>FETCH-LOGICAL-o541-c7aa3f0ad557c50b6936907f6d54347826e776cd38364ed17b4c71400ff76d9f3</originalsourceid><addsrcrecordid>eNpFjk1LwzAch4MoOKcHv8Ef751J89YeZagbDLwMLyIlzUub0SWzSRG_vQVFT7_n8OPhQeiW4BXBtLoP6diuCCvrM7QgnPGirit-_sc1vURXKR0wLjmXdIH0LoYOkg_dYOFNDadevRe9HbxWA2TlBzDxqHxI0I7edBZyb6FTJ2ht_rQ2QMrjpPM0WlDBgJuCzj4GiA6OX3H2wuv2Gl04NSR787tLtH963K83xe7lebt-2BWRM1JoqRR1WJk5THPcipqKGksnDGeUyaoUVkqhDa2oYNYQ2TItCcPYOSlM7egS3f1oY8q-Sdpnq3sdQ7A6NwRjIUv6fzqN8WOyKTeHOI1hzmrKcjZLIgj9BnKnYcg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>228367161</pqid></control><display><type>article</type><title>Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI</title><source>SpringerLink Journals</source><source>Nature</source><creator>Spink, Benjamin J ; Sivaramakrishnan, Sivaraj ; Lipfert, Jan ; Doniach, Sebastian ; Spudich, James A</creator><creatorcontrib>Spink, Benjamin J ; Sivaramakrishnan, Sivaraj ; Lipfert, Jan ; Doniach, Sebastian ; Spudich, James A ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of approximately 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the approximately 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization. [PUBLICATION ABSTRACT]</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.1429</identifier><language>eng</language><publisher>New York: Nature Publishing Group</publisher><subject>60 APPLIED LIFE SCIENCES ; ACTIN ; BASIC BIOLOGICAL SCIENCES ; Binding sites ; Biochemistry ; CARGO ; Catalysis ; DIMERIZATION ; Hypotheses ; HYPOTHESIS ; Molecular biology ; Molecular structure ; MONOMERS ; MYOSIN</subject><ispartof>Nature structural & molecular biology, 2008-09, Vol.15 (6), p.591</ispartof><rights>Copyright Nature Publishing Group Jun 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/1006723$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Spink, Benjamin J</creatorcontrib><creatorcontrib>Sivaramakrishnan, Sivaraj</creatorcontrib><creatorcontrib>Lipfert, Jan</creatorcontrib><creatorcontrib>Doniach, Sebastian</creatorcontrib><creatorcontrib>Spudich, James A</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI</title><title>Nature structural & molecular biology</title><description>Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of approximately 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the approximately 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization. [PUBLICATION ABSTRACT]</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ACTIN</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>CARGO</subject><subject>Catalysis</subject><subject>DIMERIZATION</subject><subject>Hypotheses</subject><subject>HYPOTHESIS</subject><subject>Molecular biology</subject><subject>Molecular structure</subject><subject>MONOMERS</subject><subject>MYOSIN</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpFjk1LwzAch4MoOKcHv8Ef751J89YeZagbDLwMLyIlzUub0SWzSRG_vQVFT7_n8OPhQeiW4BXBtLoP6diuCCvrM7QgnPGirit-_sc1vURXKR0wLjmXdIH0LoYOkg_dYOFNDadevRe9HbxWA2TlBzDxqHxI0I7edBZyb6FTJ2ht_rQ2QMrjpPM0WlDBgJuCzj4GiA6OX3H2wuv2Gl04NSR787tLtH963K83xe7lebt-2BWRM1JoqRR1WJk5THPcipqKGksnDGeUyaoUVkqhDa2oYNYQ2TItCcPYOSlM7egS3f1oY8q-Sdpnq3sdQ7A6NwRjIUv6fzqN8WOyKTeHOI1hzmrKcjZLIgj9BnKnYcg</recordid><startdate>20080929</startdate><enddate>20080929</enddate><creator>Spink, Benjamin J</creator><creator>Sivaramakrishnan, Sivaraj</creator><creator>Lipfert, Jan</creator><creator>Doniach, Sebastian</creator><creator>Spudich, James A</creator><general>Nature Publishing Group</general><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</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>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>OTOTI</scope></search><sort><creationdate>20080929</creationdate><title>Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI</title><author>Spink, Benjamin J ; Sivaramakrishnan, Sivaraj ; Lipfert, Jan ; Doniach, Sebastian ; Spudich, James A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-o541-c7aa3f0ad557c50b6936907f6d54347826e776cd38364ed17b4c71400ff76d9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ACTIN</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>CARGO</topic><topic>Catalysis</topic><topic>DIMERIZATION</topic><topic>Hypotheses</topic><topic>HYPOTHESIS</topic><topic>Molecular biology</topic><topic>Molecular structure</topic><topic>MONOMERS</topic><topic>MYOSIN</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spink, Benjamin J</creatorcontrib><creatorcontrib>Sivaramakrishnan, Sivaraj</creatorcontrib><creatorcontrib>Lipfert, Jan</creatorcontrib><creatorcontrib>Doniach, Sebastian</creatorcontrib><creatorcontrib>Spudich, James A</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</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>ProQuest Pharma Collection</collection><collection>Technology Research Database</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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</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 (ProQuest)</collection><collection>Environmental Sciences and Pollution Management</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>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>OSTI.GOV</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Spink, Benjamin J</au><au>Sivaramakrishnan, Sivaraj</au><au>Lipfert, Jan</au><au>Doniach, Sebastian</au><au>Spudich, James 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>Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI</atitle><jtitle>Nature structural & molecular biology</jtitle><date>2008-09-29</date><risdate>2008</risdate><volume>15</volume><issue>6</issue><spage>591</spage><pages>591-</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of approximately 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the approximately 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization. [PUBLICATION ABSTRACT]</abstract><cop>New York</cop><pub>Nature Publishing Group</pub><doi>10.1038/nsmb.1429</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1545-9993 |
| ispartof | Nature structural & molecular biology, 2008-09, Vol.15 (6), p.591 |
| issn | 1545-9993 1545-9985 |
| language | eng |
| recordid | cdi_osti_scitechconnect_1006723 |
| source | SpringerLink Journals; Nature |
| subjects | 60 APPLIED LIFE SCIENCES ACTIN BASIC BIOLOGICAL SCIENCES Binding sites Biochemistry CARGO Catalysis DIMERIZATION Hypotheses HYPOTHESIS Molecular biology Molecular structure MONOMERS MYOSIN |
| title | Long single [alpha]-helical tail domains bridge the gap between structure and function of myosin VI |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T13%3A19%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Long%20single%20%5Balpha%5D-helical%20tail%20domains%20bridge%20the%20gap%20between%20structure%20and%20function%20of%20myosin%20VI&rft.jtitle=Nature%20structural%20&%20molecular%20biology&rft.au=Spink,%20Benjamin%20J&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2008-09-29&rft.volume=15&rft.issue=6&rft.spage=591&rft.pages=591-&rft.issn=1545-9993&rft.eissn=1545-9985&rft_id=info:doi/10.1038/nsmb.1429&rft_dat=%3Cproquest_osti_%3E1492367421%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=228367161&rft_id=info:pmid/&rfr_iscdi=true |