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http://purl.uniprot.org/citations/19686686http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19686686http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19686686http://www.w3.org/2000/01/rdf-schema#comment"The spindle midzone-composed of antiparallel microtubules, microtubule-associated proteins (MAPs), and motors-is the structure responsible for microtubule organization and sliding during anaphase B. In general, MAPs and motors stabilize the midzone and motors produce sliding. We show that fission yeast kinesin-6 motor klp9p binds to the microtubule antiparallel bundler ase1p at the midzone at anaphase B onset. This interaction depends upon the phosphorylation states of klp9p and ase1p. The cyclin-dependent kinase cdc2p phosphorylates and its antagonist phosphatase clp1p dephosphorylates klp9p and ase1p to control the position and timing of klp9p-ase1p interaction. Failure of klp9p-ase1p binding leads to decreased spindle elongation velocity. The ase1p-mediated recruitment of klp9p to the midzone accelerates pole separation, as suggested by computer simulation. Our findings indicate that a phosphorylation switch controls the spatial-temporal interactions of motors and MAPs for proper anaphase B, and suggest a mechanism whereby a specific motor-MAP conformation enables efficient microtubule sliding."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2009.06.012"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2009.06.012"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Fu C."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Fu C."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Loiodice I."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Loiodice I."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Nedelec F.J."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Nedelec F.J."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Tran P.T."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Tran P.T."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Velve-Casquillas G."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Velve-Casquillas G."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Ward J.J."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/author"Ward J.J."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/pages"257-267"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/pages"257-267"xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/title"Phospho-regulated interaction between kinesin-6 Klp9p and microtubule bundler Ase1p promotes spindle elongation."xsd:string
http://purl.uniprot.org/citations/19686686http://purl.uniprot.org/core/title"Phospho-regulated interaction between kinesin-6 Klp9p and microtubule bundler Ase1p promotes spindle elongation."xsd:string