Document Detail

Ncd motor binding and transport in the spindle.
MedLine Citation:
PMID:  18957509     Owner:  NLM     Status:  MEDLINE    
The Ncd kinesin-14 motor is required for meiotic spindle assembly in Drosophila oocytes and produces force in mitotic spindles that opposes other motors. Despite extensive studies, the way the motor binds to the spindle to perform its functions is not well understood. By analyzing Ncd deleted for the conserved head or the positively charged tail, we found that the tail is essential for binding to spindles and centrosomes, but both the head and tail are needed for normal spindle assembly and function. Fluorescence photobleaching assays to analyze binding interactions with the spindle yielded data for headless and full-length Ncd that did not fit well to previous recovery models. We report a new model that accounts for Ncd transport towards the equator revealed by fluorescence flow analysis of early mitotic spindles and gives rate constants that confirm the dominant role the Ncd tail plays in binding to the spindle. By contrast, the head binds weakly to spindles based on analysis of the tailless fluorescence recovery data. Minus-end Ncd thus binds tightly to spindles and is transported in early metaphase towards microtubule plus-ends, the opposite direction to that in which the motor moves, to produce force in the spindle later in mitosis.
Mark A Hallen; Zhang-Yi Liang; Sharyn A Endow
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-10-28
Journal Detail:
Title:  Journal of cell science     Volume:  121     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-11-06     Completed Date:  2009-06-04     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  3834-41     Citation Subset:  IM    
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MeSH Terms
Amino Acid Motifs
Drosophila / chemistry,  cytology,  genetics,  metabolism*
Drosophila Proteins / chemistry*,  genetics,  metabolism*
Kinesin / chemistry*,  genetics,  metabolism*
Oocytes / chemistry,  cytology,  metabolism
Protein Binding
Protein Transport
Spindle Apparatus / genetics,  metabolism*
Grant Support
Reg. No./Substance:
0/Drosophila Proteins; 0/ncd protein, Drosophila; EC 3.6.1.-/Kinesin

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

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