Document Detail


The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis.
MedLine Citation:
PMID:  12015116     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Mitotic chromosome segregation depends on bi-orientation and capture of sister kinetochores by microtubules emanating from opposite spindle poles and the near synchronous loss of sister chromatid cohesion. During meiosis I, in contrast, sister kinetochores orient to the same pole, and homologous kinetochores are captured by microtubules emanating from opposite spindle poles. Additionally, mechanisms exist that prevent complete loss of cohesion during meiosis I. These features ensure that homologs separate during meiosis I and sister chromatids remain together until meiosis II. The mechanisms responsible for orienting kinetochores in mitosis and for causing asynchronous loss of cohesion during meiosis are not well understood.
RESULTS: During mitosis in C. elegans, aurora B kinase, AIR-2, is not required for sister chromatid separation, but it is required for chromosome segregation. Condensin recruitment during metaphase requires AIR-2; however, condensin functions during prometaphase, independent of AIR-2. During metaphase, AIR-2 promotes chromosome congression to the metaphase plate, perhaps by inhibiting attachment of chromatids to both spindle poles. During meiosis in AIR-2-depleted oocytes, congression of bivalents appears normal, but segregation fails. Localization of AIR-2 on meiotic bivalents suggests this kinase promotes separation of homologs by promoting the loss of cohesion distal to the single chiasma. Inactivation of the phosphatase that antagonizes AIR-2 causes premature separation of chromatids during meiosis I, in a separase-dependent reaction.
CONCLUSIONS: Aurora B functions to resolve chiasmata during meiosis I and to regulate kinetochore function during mitosis. Condensin mediates chromosome condensation during prophase, and condensin-independent pathways contribute to chromosome condensation during metaphase.
Authors:
Susanne Kaitna; Pawel Pasierbek; Michael Jantsch; Josef Loidl; Michael Glotzer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Current biology : CB     Volume:  12     ISSN:  0960-9822     ISO Abbreviation:  Curr. Biol.     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-05-16     Completed Date:  2002-10-17     Revised Date:  2011-07-11    
Medline Journal Info:
Nlm Unique ID:  9107782     Medline TA:  Curr Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  798-812     Citation Subset:  IM    
Affiliation:
Research Institute of Molecular Pathology (IMP), Dr. Bohr-Gasse 7, A-1030, Vienna, Austria.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / deficiency,  genetics,  metabolism
Animals
Caenorhabditis elegans / cytology*,  embryology,  enzymology*,  genetics
Caenorhabditis elegans Proteins / genetics,  metabolism
Chromatids / chemistry,  genetics,  physiology
Chromosome Segregation*
DNA-Binding Proteins / deficiency,  genetics,  metabolism
Embryo, Nonmammalian / cytology,  enzymology,  metabolism
Epitopes
Helminth Proteins / metabolism
Histones / metabolism
In Situ Hybridization, Fluorescence
Kinetochores / enzymology*
Meiosis*
Metaphase
Mitosis*
Models, Biological
Multiprotein Complexes
Mutation
Phosphoproteins / metabolism
Protein Binding
Protein-Serine-Threonine Kinases / deficiency,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/BIR1 protein, C elegans; 0/Caenorhabditis elegans Proteins; 0/DNA-Binding Proteins; 0/Epitopes; 0/Helminth Proteins; 0/Histones; 0/Multiprotein Complexes; 0/Phosphoproteins; 0/condensin complexes; EC 2.7.1.-/AIR-2 protein, C elegans; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/aurora kinase; EC 3.6.1.-/Adenosine Triphosphatases
Comments/Corrections
Comment In:
Curr Biol. 2002 Jul 9;12(13):R458-60   [PMID:  12121637 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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