title: Cleavage of cohesin rings coordinates the separation of centrioles and chromatids.
abstract: Cohesin pairs sister chromatids by forming a tripartite Scc1-Smc1-Smc3 ring around them. In mitosis, cohesin is removed from chromosome arms by the phosphorylation-dependent prophase pathway. Centromeric cohesin is protected by shugoshin 1 and protein phosphatase 2A (Sgo1-PP2A) and opened only in anaphase by separase-dependent cleavage of Scc1 (refs 4-6). Following chromosome segregation, centrioles loosen their tight orthogonal arrangement, which licenses later centrosome duplication in S phase. Although a role of separase in centriole disengagement has been reported, the molecular details of this process remain enigmatic. Here, we identify cohesin as a centriole-engagement factor. Both premature sister-chromatid separation and centriole disengagement are induced by ectopic activation of separase or depletion of Sgo1. These unscheduled events are suppressed by expression of non-cleavable Scc1 or inhibition of the prophase pathway. When endogenous Scc1 is replaced by artificially cleavable Scc1, the corresponding site-specific protease triggers centriole disengagement. Separation of centrioles can alternatively be induced by ectopic cleavage of an engineered Smc3. Thus, the chromosome and centrosome cycles exhibit extensive parallels and are coordinated with each other by dual use of the cohesin ring complex.
authors: University of Bayreuth, 95440 Bayreuth, Germany.
authors: Laura
authors: L
authors: Schöckel
authors: Martin
authors: M
authors: Möckel
authors: Bernd
authors: B
authors: Mayer
authors: Dominik
authors: D
authors: Boos
authors: Olaf
authors: O
authors: Stemmann
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000502:physiology*; D002502:Centrioles / Q000502:physiology*; D002842:Chromatids / Q000502:physiology*; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry / Q000502:physiology*; D004268:DNA-Binding Proteins; D010450:Endopeptidases / Q000502:physiology; D005260:Female; D057809:HEK293 Cells; D006801:Humans; D066298:In Vitro Techniques; D008954:Models, Biological; D046912:Multiprotein Complexes; D009687:Nuclear Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000502:physiology; D010750:Phosphoproteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000502:physiology; D034741:RNA, Small Interfering / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D064247:Separase; D014162:Transfection; D029867:Xenopus Proteins / Q000502:physiology; D014982:Xenopus laevis; D000097722:Cohesins
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D010450:Endopeptidases; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D010750:Phosphoproteins; D034741:RNA, Small Interfering; D011994:Recombinant Proteins; D064247:Separase; D029867:Xenopus Proteins; D000097722:Cohesins; C429022:RAD21 protein, human; C577987:ESPL1 protein, human