Document Detail

Looping in on Ndc80 - How does a protein loop at the kinetochore control chromosome segregation?
MedLine Citation:
PMID:  23154893     Owner:  NLM     Status:  In-Data-Review    
Segregation of chromosomes during mitosis requires the interaction of dynamic microtubules with the kinetochore, a large protein structure established on the centromere region of sister chromatids. The core microtubule-binding activity of the kinetochore resides in the KMN network, an outer kinetochore complex. As part of the KMN network, the Ndc80 complex, which is composed of Ndc80, Nuf2, Spc24, and Spc25, is able to bind directly to microtubules and has the ability to track with depolymerizing microtubules to produce chromosome movement. The Ndc80 complex binds directly to microtubules through a calponin homology domain and an unstructured tail in the N terminus of the Ndc80 protein. A recent flurry of papers has highlighted the importance of an internal loop region in Ndc80 in establishing end-on attachment to microtubules. Here I discuss these recent findings that suggest that the Ndc80 internal loop functions as a binding site for proteins required for kinetochore-microtubule interactions.
Jakob Nilsson
Related Documents :
11395483 - The uptake inhibitors cocaine and benztropine differentially alter the conformation of ...
8684623 - Quantitative autoradiography reveals regionally selective changes in dopamine d1 and d2...
8086403 - Structure of the extracellular domain of human tissue factor: location of the factor vi...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  BioEssays : news and reviews in molecular, cellular and developmental biology     Volume:  34     ISSN:  1521-1878     ISO Abbreviation:  Bioessays     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8510851     Medline TA:  Bioessays     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1070-7     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 WILEY Periodicals, Inc.
The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Science, University of Copenhagen, Copenhagen, Denmark.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  High-Voltage Pyrophosphate Cathode: Insights into Local Structure and Lithium-Diffusion Pathways.
Next Document:  Comparison of Goldmann applanation and dynamic contour tonometry in a population of Mexican open-ang...