Structure of the dynein-2 complex and its assembly with intraflagellar transport trains
Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical...
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| Veröffentlicht in: | Nature structural & molecular biology 2019-09, Vol.26 (9), p.823-829 |
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| creator | Toropova, Katerina Zalyte, Ruta Mukhopadhyay, Aakash G. Mladenov, Miroslav Carter, Andrew P. Roberts, Anthony J. |
| description | Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60−WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60−WDR34−light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.
Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains. |
| doi_str_mv | 10.1038/s41594-019-0286-y |
| format | Article |
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Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-019-0286-y</identifier><identifier>PMID: 31451806</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/45/535/1258/1259 ; 631/57/343/2277 ; 631/80/128/1383 ; 631/80/128/1441 ; Assembly ; Asymmetry ; Atomic structure ; Axonal transport ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Cilia ; Conformation ; Cryoelectron Microscopy ; Dynein ; Dyneins - metabolism ; Dyneins - ultrastructure ; Gene mutations ; Humans ; Life Sciences ; Light ; Light chains ; Membrane Biology ; Molecular biology ; Molecular conformation ; Periodicity ; Protein Conformation ; Protein Multimerization ; Protein Structure ; Protein Transport ; Stoichiometry ; Symmetry ; Transport</subject><ispartof>Nature structural & molecular biology, 2019-09, Vol.26 (9), p.823-829</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2019</rights><rights>COPYRIGHT 2019 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Sep 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c571t-469dce9609380545c90f8f77a8d260a7fede45ea1da0649e10183a482c9196353</citedby><cites>FETCH-LOGICAL-c571t-469dce9609380545c90f8f77a8d260a7fede45ea1da0649e10183a482c9196353</cites><orcidid>0000-0001-5277-6730</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41594-019-0286-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41594-019-0286-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31451806$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Toropova, Katerina</creatorcontrib><creatorcontrib>Zalyte, Ruta</creatorcontrib><creatorcontrib>Mukhopadhyay, Aakash G.</creatorcontrib><creatorcontrib>Mladenov, Miroslav</creatorcontrib><creatorcontrib>Carter, Andrew P.</creatorcontrib><creatorcontrib>Roberts, Anthony J.</creatorcontrib><title>Structure of the dynein-2 complex and its assembly with intraflagellar transport trains</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60−WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60−WDR34−light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.
Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains.</description><subject>631/45/535/1258/1259</subject><subject>631/57/343/2277</subject><subject>631/80/128/1383</subject><subject>631/80/128/1441</subject><subject>Assembly</subject><subject>Asymmetry</subject><subject>Atomic structure</subject><subject>Axonal transport</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cilia</subject><subject>Conformation</subject><subject>Cryoelectron Microscopy</subject><subject>Dynein</subject><subject>Dyneins - metabolism</subject><subject>Dyneins - ultrastructure</subject><subject>Gene mutations</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Light</subject><subject>Light 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Biol</addtitle><date>2019-09-01</date><risdate>2019</risdate><volume>26</volume><issue>9</issue><spage>823</spage><epage>829</epage><pages>823-829</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60−WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60−WDR34−light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family.
Cryo-EM structure of the dynein-2 complex (involved in intraflagellar transport, IFT) reveals distinct conformations of the two DHC2 tails within the same assembly, suggesting the mechanisms of autoinhibition and of transport on anterograde IFT trains.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>31451806</pmid><doi>10.1038/s41594-019-0286-y</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0001-5277-6730</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 631/45/535/1258/1259 631/57/343/2277 631/80/128/1383 631/80/128/1441 Assembly Asymmetry Atomic structure Axonal transport Biochemistry Biological Microscopy Biomedical and Life Sciences Cilia Conformation Cryoelectron Microscopy Dynein Dyneins - metabolism Dyneins - ultrastructure Gene mutations Humans Life Sciences Light Light chains Membrane Biology Molecular biology Molecular conformation Periodicity Protein Conformation Protein Multimerization Protein Structure Protein Transport Stoichiometry Symmetry Transport |
| title | Structure of the dynein-2 complex and its assembly with intraflagellar transport trains |
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