title: Bub1 and Bub3 promote the conversion from monopolar to bipolar chromosome attachment independently of shugoshin.
abstract: The eukaryotic spindle assembly checkpoint (SAC) delays anaphase in the presence of chromosome attachment errors. Bub3 has been reported to be required for SAC activity in all eukaryotes examined so far. We find that Bub3, unlike its binding partner Bub1, is not essential for the SAC in fission yeast. As Bub3 is needed for the efficient kinetochore localization of Bub1, and of Mad1, Mad2 and Mad3, this implies that most SAC proteins do not need to be enriched at the kinetochores for the SAC to function. We find that Bub3 is also dispensable for shugoshin localization to the centromeres, which is the second known function of Bub1. Instead, Bub3, together with Bub1, has a specific function in promoting the conversion from chromosome mono-orientation to bi-orientation.
authors.affiliation: Friedrich Miescher Laboratory of the Max Planck Society, Spemannstrasse 39, 72076 Tuebingen, Germany.
authors.forename: Hanna
authors.initials: H
authors.lastname: Windecker
authors.forename: Maria
authors.initials: M
authors.lastname: Langegger
authors.forename: Stephanie
authors.initials: S
authors.lastname: Heinrich
authors.forename: Silke
authors.initials: S
authors.lastname: Hauf
mesh_terms: D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000235:genetics / Q000378:metabolism; D020090:Chromosome Segregation; D015825:Chromosomes, Fungal / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D008941:Spindle Apparatus / Q000378:metabolism
chemical_list: C544653:Bub3 protein, S pombe; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D029702:Schizosaccharomyces pombe Proteins; C485974:Sgo2 protein, S pombe; C495594:Bub1 protein, S pombe; D017346:Protein Serine-Threonine Kinases
references.citation: Mol Cell Biol. 2002 Apr;22(8):2728-42
references.pmid: 11909965
references.citation: Genes Dev. 2000 Sep 15;14(18):2277-82
references.pmid: 10995385
references.citation: J Cell Biol. 2003 Apr 28;161(2):267-80
references.pmid: 12719470
references.citation: Genetics. 2008 Jun;179(2):785-92
references.pmid: 18505884
references.citation: Genes Dev. 2008 Sep 1;22(17):2385-99
references.pmid: 18765790
references.citation: Nat Rev Mol Cell Biol. 2002 Oct;3(10):731-41
references.pmid: 12360190
references.citation: Nat Rev Mol Cell Biol. 2006 Sep;7(9):644-56
references.pmid: 16896351
references.citation: Genetics. 1998 May;149(1):101-16
references.pmid: 9584089
references.citation: J Cell Biol. 1998 Dec 14;143(6):1603-16
references.pmid: 9852154
references.citation: Mol Biol Cell. 2008 Apr;19(4):1646-62
references.pmid: 18256284
references.citation: J Cell Biol. 2006 Jul 3;174(1):39-51
references.pmid: 16818718
references.citation: Mol Biol Cell. 2007 Jun;18(6):2216-25
references.pmid: 17409356
references.citation: Mol Biol Cell. 2008 Mar;19(3):1199-209
references.pmid: 18094053
references.citation: Mol Biol Cell. 2007 May;18(5):1657-69
references.pmid: 17301288
references.citation: J Cell Sci. 2005 Jan 1;118(Pt 1):187-98
references.pmid: 15615783
references.citation: Methods Enzymol. 1991;194:795-823
references.pmid: 2005825
references.citation: Mol Biol Cell. 2005 Jan;16(1):385-95
references.pmid: 15525673
references.citation: Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1201-6
references.pmid: 17227844
references.citation: Science. 2006 Jan 20;311(5759):388-91
references.pmid: 16424343
references.citation: J Cell Biol. 2009 Jun 1;185(5):841-58
references.pmid: 19487456
references.citation: Mol Biol Cell. 2008 Apr;19(4):1798-813
references.pmid: 18199686
references.citation: Science. 2005 Jan 7;307(5706):130-3
references.pmid: 15637284
references.citation: EMBO J. 2006 Oct 18;25(20):4888-96
references.pmid: 17036054
references.citation: Mol Biol Cell. 1999 Aug;10(8):2771-85
references.pmid: 10436027
references.citation: J Cell Sci. 2003 Feb 15;116(Pt 4):617-28
references.pmid: 12538762
references.citation: PLoS Genet. 2007 Nov;3(11):e213
references.pmid: 18081426
references.citation: Dev Cell. 2009 Jan;16(1):105-17
references.pmid: 19154722
references.citation: EMBO J. 2007 Oct 31;26(21):4475-86
references.pmid: 17932486
references.citation: J Biol Chem. 2007 Apr 13;282(15):11205-12
references.pmid: 17289665
references.citation: EMBO J. 2005 Apr 20;24(8):1621-33
references.pmid: 15933723
references.citation: Mol Biol Cell. 2009 Feb;20(4):1252-67
references.pmid: 19109417
references.citation: PLoS Biol. 2009 Jan 13;7(1):e10
references.pmid: 19143472
references.citation: Mol Cell Biol. 2004 Nov;24(22):9786-801
references.pmid: 15509783
references.citation: Cell. 1991 Aug 9;66(3):507-17
references.pmid: 1651171
references.citation: J Cell Biol. 1998 Dec 28;143(7):1775-87
references.pmid: 9864354
references.citation: Cell. 1984 Dec;39(2 Pt 1):349-58
references.pmid: 6094012
references.citation: Nat Cell Biol. 2008 Dec;10(12):1411-20
references.pmid: 18997788
references.citation: Dev Cell. 2004 Jul;7(1):45-60
references.pmid: 15239953
references.citation: J Cell Sci. 1995 Mar;108 ( Pt 3):1195-204
references.pmid: 7622604
references.citation: Genes Dev. 2007 Feb 15;21(4):420-35
references.pmid: 17322402
references.citation: Nature. 2004 Feb 5;427(6974):510-7
references.pmid: 14730319
references.citation: J Cell Sci. 2007 Oct 1;120(Pt 19):3345-51
references.pmid: 17881496
references.citation: Mol Biol Cell. 2002 Sep;13(9):3029-41
references.pmid: 12221113
references.citation: Curr Biol. 2005 Feb 8;15(3):214-25
references.pmid: 15694304
references.citation: Nat Cell Biol. 2005 Jan;7(1):93-8
references.pmid: 15592459
references.citation: Nat Rev Mol Cell Biol. 2007 May;8(5):379-93
references.pmid: 17426725