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http://purl.uniprot.org/citations/17804403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17804403http://www.w3.org/2000/01/rdf-schema#comment"Stabilization of spindle microtubules during anaphase is essential for proper chromosome segregation. Fin1 is a budding yeast protein that localizes to the poles and microtubules of the spindle during anaphase and contributes to spindle stability. The N-terminal half of Fin1 is phosphorylated at multiple sites by the cyclin-dependent kinase Clb5-Cdk1, and dephosphorylation in anaphase triggers its localization to the spindle. The C-terminal half of Fin1 contains coiled-coil motifs that are required for its self-association. Here we investigated the functional importance of the two regions of Fin1. Fin1 mutants lacking the C-terminal coiled-coil domains localized to spindle pole bodies but not along spindle microtubules. These mutants failed to self-associate and displayed reduced binding to microtubules in vitro but were functional in vivo and stabilized anaphase spindles when dephosphorylated. Deletion of the Fin1 C terminus suppressed the lethal phenotypes of the phospho-mutant Fin15A. Our findings suggest that the N-terminal region of Fin1 is sufficient for its regulated function as a spindle-stabilizing factor and that this function involves association with the spindle pole body. The ability of the C-terminal region to promote Fin1 self-association and microtubule binding may underlie the lethal effects of the deregulated Fin15A mutant."xsd:string
http://purl.uniprot.org/citations/17804403http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m705344200"xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/author"Morgan D.O."xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/author"Woodbury E.L."xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/pages"32138-32143"xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/title"The role of self-association in Fin1 function on the mitotic spindle."xsd:string
http://purl.uniprot.org/citations/17804403http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17804403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17804403
http://purl.uniprot.org/citations/17804403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17804403
http://purl.uniprot.org/uniprot/Q03898#attribution-CE8978E151A751044DF4C02B6BDC9FEChttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17804403
http://purl.uniprot.org/uniprot/Q03898#attribution-F1D593A722C6B87EBEC823FD3F936C93http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17804403
http://purl.uniprot.org/uniprot/#_A0A8H8UN43-mappedCitation-17804403http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17804403
http://purl.uniprot.org/uniprot/#_Q03898-mappedCitation-17804403http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17804403
http://purl.uniprot.org/uniprot/A0A8H8UN43http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17804403
http://purl.uniprot.org/uniprot/Q03898http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17804403