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http://purl.uniprot.org/citations/26437877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26437877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26437877http://www.w3.org/2000/01/rdf-schema#comment"Kinesin-5 slides antiparallel microtubules during spindle assembly, and regulates the branching of growing axons. Besides the mechanical activities enabled by its tetrameric configuration, the specific motor properties of kinesin-5 that underlie its cellular function remain unclear. Here by engineering a stable kinesin-5 dimer and reconstituting microtubule dynamics in vitro, we demonstrate that kinesin-5 promotes microtubule polymerization by increasing the growth rate and decreasing the catastrophe frequency. Strikingly, microtubules growing in the presence of kinesin-5 have curved plus ends, suggesting that the motor stabilizes growing protofilaments. Single-molecule fluorescence experiments reveal that kinesin-5 remains bound to the plus ends of static microtubules for 7 s, and tracks growing microtubule plus ends in a manner dependent on its processivity. We propose that kinesin-5 pauses at microtubule plus ends and enhances polymerization by stabilizing longitudinal tubulin-tubulin interactions, and that these activities underlie the ability kinesin-5 to slide and stabilize microtubule bundles in cells."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.org/dc/terms/identifier"doi:10.1038/ncomms9160"xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/author"Hancock W.O."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/author"Hancock W.O."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/pages"8160"xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/pages"8160"xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/title"Kinesin-5 is a microtubule polymerase."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/title"Kinesin-5 is a microtubule polymerase."xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/26437877http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/26437877http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26437877
http://purl.uniprot.org/citations/26437877http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26437877
http://purl.uniprot.org/citations/26437877http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26437877
http://purl.uniprot.org/citations/26437877http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26437877
http://purl.uniprot.org/uniprot/Q8AVK8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/26437877
http://purl.uniprot.org/uniprot/#_Q8AVK8-citation-26437877http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26437877
http://purl.uniprot.org/uniprot/#_Q0PQ30-mappedCitation-26437877http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26437877