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http://purl.uniprot.org/citations/20946984http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20946984http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20946984http://www.w3.org/2000/01/rdf-schema#comment"Tubulin assembles into microtubule polymers that have distinct plus and minus ends. Most microtubule plus ends in living cells are dynamic; the transitions between growth and shrinkage are regulated by assembly-promoting and destabilizing proteins. In contrast, minus ends are generally not dynamic, suggesting their stabilization by some unknown protein. Here, we have identified Patronin (also known as ssp4) as a protein that stabilizes microtubule minus ends in Drosophila S2 cells. In the absence of Patronin, minus ends lose subunits through the actions of the Kinesin-13 microtubule depolymerase, leading to a sparse interphase microtubule array and short, disorganized mitotic spindles. In vitro, the selective binding of purified Patronin to microtubule minus ends is sufficient to protect them against Kinesin-13-induced depolymerization. We propose that Patronin caps and stabilizes microtubule minus ends, an activity that serves a critical role in the organization of the microtubule cytoskeleton."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2010.09.022"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2010.09.022"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/author"Vale R.D."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/author"Vale R.D."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/author"Goodwin S.S."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/author"Goodwin S.S."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/pages"263-274"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/pages"263-274"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/title"Patronin regulates the microtubule network by protecting microtubule minus ends."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/title"Patronin regulates the microtubule network by protecting microtubule minus ends."xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/volume"143"xsd:string
http://purl.uniprot.org/citations/20946984http://purl.uniprot.org/core/volume"143"xsd:string
http://purl.uniprot.org/citations/20946984http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20946984
http://purl.uniprot.org/citations/20946984http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20946984
http://purl.uniprot.org/citations/20946984http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20946984
http://purl.uniprot.org/citations/20946984http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20946984
http://purl.uniprot.org/uniprot/O97143http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20946984
http://purl.uniprot.org/uniprot/A1ZAU8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20946984