Document Detail

Ringing the changes: emerging roles for DASH at the kinetochore-microtubule Interface.
MedLine Citation:
PMID:  21271286     Owner:  NLM     Status:  MEDLINE    
Regulated interaction between kinetochores and the mitotic spindle is essential for the fidelity of chromosome segregation. Potentially deleterious attachments are corrected during prometaphase and metaphase. Correct attachments must persist during anaphase, when spindle-generated forces separate chromosomes to opposite poles. In yeast, the heterodecameric DASH complex plays a vital pole in maintaining this link. In vitro DASH forms both oligomeric patches and rings that can form load-bearing attachments with the tips of polymerising and depolymerising microtubules. In vivo, DASH localises primarily at the kinetochore, and has a role maintaining correct attachment between spindles and chromosomes in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. Recent work has begun to describe how DASH acts alongside other components of the outer kinetochore to create a dynamic, regulated kinetochore-microtubule interface. Here, we review some of the key experiments into DASH function and discuss their implications for the nature of kinetochore-microtubule attachments in yeast and other organisms.
Graham J Buttrick; Jonathan B A Millar
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology     Volume:  19     ISSN:  1573-6849     ISO Abbreviation:  Chromosome Res.     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-04-18     Completed Date:  2011-07-29     Revised Date:  2014-02-20    
Medline Journal Info:
Nlm Unique ID:  9313452     Medline TA:  Chromosome Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  393-407     Citation Subset:  IM    
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MeSH Terms
Kinetochores / metabolism*
Microtubule-Associated Proteins / chemistry,  metabolism*
Microtubules / metabolism*
Nuclear Proteins / metabolism
Protein Binding
Yeasts / metabolism
Grant Support
G0601118//Medical Research Council
Reg. No./Substance:
0/Microtubule-Associated Proteins; 0/Nuclear Proteins

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

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