title: A Bir1p Sli15p kinetochore passenger complex regulates septin organization during anaphase.
abstract: Kinetochore-passenger complexes in metazoans have been proposed to coordinate the segregation of chromosomes in anaphase with the induction of cytokinesis. Passenger protein homologues in the budding yeast Saccharomyces cerevisiae play a critical role early in mitosis, ensuring proper biorientation of kinetochore-microtubule attachments. Our recent work has implicated the passenger protein Bir1p (Survivin) and the inner kinetochore complex centromere binding factor 3 (CBF3) in the regulation of septin dynamics during anaphase. Here, we present data that is consistent with there being multiple passenger protein complexes. Our data show that Bir1p links together a large passenger complex containing Ndc10p, Sli15p (INCENP), and Ipl1p (Aurora B) and that the interaction between Bir1p and Sli15p is specifically involved in regulating septin dynamics during anaphase. Neither conditional alleles nor mutants of BIR1 that disrupt the interaction between Bir1p and Sli15p resulted in mono-attached kinetochores, suggesting that the Bir1p-Sli15p complex functions in anaphase and independently from Sli15p-Ipl1p complexes. We present a model for how discrete passenger complexes coordinate distinct aspects of mitosis.
authors.affiliation: Section of Molecular and Cellular Biology, University of California at Davis, Davis, CA 95616, USA.
authors.forename: Scott
authors.initials: S
authors.lastname: Thomas
authors.forename: Kenneth B
authors.initials: KB
authors.lastname: Kaplan
mesh_terms: D000595:Amino Acid Sequence; D000705:Anaphase; D049109:Cell Proliferation; D020090:Chromosome Segregation; D048749:Cytokinesis; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D018386:Kinetochores / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000166:cytology* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D008941:Spindle Apparatus / Q000378:metabolism; D020798:Two-Hybrid System Techniques
chemical_list: D005656:Fungal Proteins; D008869:Microtubule-Associated Proteins; D046912:Multiprotein Complexes; D029701:Saccharomyces cerevisiae Proteins; C480084:Sli15 protein, S cerevisiae